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Stromal cell-derived factor 1 (SDF-1) (hSDF-1) (C-X-C motif chemokine 12) (Intercrine reduced in hepatomas) (IRH) (hIRH) (Pre-B cell growth-stimulating factor) (PBSF) [Cleaved into: SDF-1-beta(3-72); SDF-1-alpha(3-67)]

 SDF1_HUMAN              Reviewed;          93 AA.
P48061; B2R4G0; E7EVL0; H7BYN8; Q2L985; Q2L986; Q2L988; Q5IT36;
Q6ICW0; Q9H554;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 186.
RecName: Full=Stromal cell-derived factor 1;
Short=SDF-1;
Short=hSDF-1;
AltName: Full=C-X-C motif chemokine 12;
AltName: Full=Intercrine reduced in hepatomas;
Short=IRH;
Short=hIRH;
AltName: Full=Pre-B cell growth-stimulating factor;
Short=PBSF;
Contains:
RecName: Full=SDF-1-beta(3-72);
Contains:
RecName: Full=SDF-1-alpha(3-67);
Flags: Precursor;
Name=CXCL12; Synonyms=SDF1, SDF1A, SDF1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
PubMed=7490086; DOI=10.1006/geno.1995.1180;
Shirozu M., Nakano T., Inazawa J., Tashiro K., Tada H., Shinohara T.,
Honjo T.;
"Structure and chromosomal localization of the human stromal cell-
derived factor 1 (SDF1) gene.";
Genomics 28:495-500(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA; DELTA; EPSILON AND THETA),
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
TISSUE=Fetal brain, Fetal heart, and Heart;
PubMed=16626895; DOI=10.1016/j.gene.2006.02.001;
Yu L., Cecil J., Peng S.B., Schrementi J., Kovacevic S., Paul D.,
Su E.W., Wang J.;
"Identification and expression of novel isoforms of human stromal
cell-derived factor 1.";
Gene 374:174-179(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
TISSUE=Fibroblast;
Spotila L.D.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Liver;
Begum N.A., Barnard G.F.;
"Nucleotide sequence of hIRH, human intercrine reduced in hepatomas.";
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA).
Callebaut C., Verdin E.;
"Inhibition of X4 and R5 HIV-1 by human SDF-1g, a novel chemokine that
interferes with HIV transcription.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Zhao X., Zhang H., Lee S., Wong K., Zheng B.;
"Polymorphism study of cell-derived factor 1 (SDF1) gene and their
correlation with HIV infection in a Chinese cohort.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=Thymus, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
PubMed=16344560; DOI=10.1101/gr.4039406;
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
"Diversification of transcriptional modulation: large-scale
identification and characterization of putative alternative promoters
of human genes.";
Genome Res. 16:55-65(2006).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
FUNCTION.
PubMed=8752281; DOI=10.1038/382833a0;
Oberlin E., Amara A., Bachelerie F., Bessia C., Virelizier J.-L.,
Arenzana-Seisdedos F., Schwartz O., Heard J.-M., Clark-Lewis I.,
Legler D.F., Loetscher M., Baggiolini M., Moser B.;
"The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents
infection by T-cell-line-adapted HIV-1.";
Nature 382:833-835(1996).
[15]
INTERACTION WITH CXCR4.
PubMed=9427609; DOI=10.1038/nm0198-072;
Donzella G.A., Schols D., Lin S.W., Este J.A., Nagashima K.A.,
Maddon P.J., Allaway G.P., Sakmar T.P., Henson G., De Clercq E.,
Moore J.P.;
"AMD3100, a small molecule inhibitor of HIV-1 entry via the CXCR4 co-
receptor.";
Nat. Med. 4:72-77(1998).
[16]
INTERACTION WITH HEPARAN SULFATE, AND MUTAGENESIS OF 45-LYS--LYS-48.
PubMed=10446158; DOI=10.1074/jbc.274.34.23916;
Amara A., Lorthioir O., Valenzuela A., Magerus A., Thelen M.,
Montes M., Virelizier J.L., Delepierre M., Baleux F., Lortat-Jacob H.,
Arenzana-Seisdedos F.;
"Stromal cell-derived factor-1alpha associates with heparan sulfates
through the first beta-strand of the chemokine.";
J. Biol. Chem. 274:23916-23925(1999).
[17]
FUNCTION.
PubMed=11069075;
DOI=10.1002/1521-4141(200010)30:10<2924::AID-IMMU2924>3.0.CO;2-Y;
Moepps B., Braun M., Knoepfle K., Dillinger K., Knoechel W.,
Gierschik P.;
"Characterization of a Xenopus laevis CXC chemokine receptor 4:
implications for hematopoietic cell development in the vertebrate
embryo.";
Eur. J. Immunol. 30:2924-2934(2000).
[18]
FUNCTION.
PubMed=11859124; DOI=10.4049/jimmunol.168.5.2340;
Braun M., Wunderlin M., Spieth K., Knoechel W., Gierschik P.,
Moepps B.;
"Xenopus laevis stromal cell-derived factor 1: conservation of
structure and function during vertebrate development.";
J. Immunol. 168:2340-2347(2002).
[19]
IDENTIFICATION OF SDF-1ALPHA(3-67) AND SDF-1BETA(3-72) BY MASS
SPECTROMETRY, AND PROTEOLYTIC PROCESSING OF N-TERMINUS AND C-TERMINUS.
PubMed=14525775; DOI=10.1182/blood-2003-08-2857;
De La Luz Sierra M., Yang F., Narazaki M., Salvucci O., Davis D.,
Yarchoan R., Zhang H.H., Fales H., Tosato G.;
"Differential processing of stromal-derived factor-1alpha and beta
explains functional diversity.";
Blood 103:2452-2459(2004).
[20]
FUNCTION, AND INTERACTION WITH ACKR3.
PubMed=16107333; DOI=10.1074/jbc.M508234200;
Balabanian K., Lagane B., Infantino S., Chow K.Y., Harriague J.,
Moepps B., Arenzana-Seisdedos F., Thelen M., Bachelerie F.;
"The chemokine SDF-1/CXCL12 binds to and signals through the orphan
receptor RDC1 in T lymphocytes.";
J. Biol. Chem. 280:35760-35766(2005).
[21]
DIMERIZATION, AND MUTAGENESIS OF HIS-46.
PubMed=15741341; DOI=10.1110/ps.041219505;
Veldkamp C.T., Peterson F.C., Pelzek A.J., Volkman B.F.;
"The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL
12) is altered by pH, phosphate, sulfate, and heparin.";
Protein Sci. 14:1071-1081(2005).
[22]
DIMERIZATION, AND INTERACTION WITH CXCR4.
PubMed=16725153; DOI=10.1016/j.jmb.2006.04.052;
Veldkamp C.T., Seibert C., Peterson F.C., Sakmar T.P., Volkman B.F.;
"Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-
derived factor-1alpha (SDF-1alpha/CXCL12).";
J. Mol. Biol. 359:1400-1409(2006).
[23]
FUNCTION.
PubMed=18802065; DOI=10.4049/jimmunol.181.7.4632;
Malik M., Chen Y.-Y., Kienzle M.F., Tomkowicz B.E., Collman R.G.,
Ptasznik A.;
"Monocyte migration and LFA-1-mediated attachment to brain
microvascular endothelia is regulated by SDF-1 alpha through Lyn
kinase.";
J. Immunol. 181:4632-4637(2008).
[24]
FUNCTION, AND INTERACTION WITH ACKR3.
PubMed=19255243; DOI=10.1124/mol.108.053389;
Kalatskaya I., Berchiche Y.A., Gravel S., Limberg B.J.,
Rosenbaum J.S., Heveker N.;
"AMD3100 is a CXCR7 ligand with allosteric agonist properties.";
Mol. Pharmacol. 75:1240-1247(2009).
[25]
RECEPTOR INTERACTION.
PubMed=22457824; DOI=10.1371/journal.pone.0034192;
Canals M., Scholten D.J., de Munnik S., Han M.K., Smit M.J., Leurs R.;
"Ubiquitination of CXCR7 controls receptor trafficking.";
PLoS ONE 7:E34192-E34192(2012).
[26]
STRUCTURE BY NMR OF 22-88, DISULFIDE BONDS, AND MUTAGENESIS OF LYS-22;
PRO-23; 22-LYS-PRO-23; 25-SER--SER-27; TYR-28 AND ARG-29.
PubMed=9384579; DOI=10.1093/emboj/16.23.6996;
Crump M.P., Gong J.H., Loetscher P., Rajarathnam K., Amara A.,
Arenzana-Seisdedos F., Virelizier J.-L., Baggiolini M., Sykes B.D.,
Clark-Lewis I.;
"Solution structure and basis for functional activity of stromal cell-
derived factor-1; dissociation of CXCR4 activation from binding and
inhibition of HIV-1.";
EMBO J. 16:6996-7007(1997).
[27]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-88 OF MUTANT ALA-54, AND
DISULFIDE BONDS.
PubMed=9618518; DOI=10.1073/pnas.95.12.6941;
Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A.,
Lolis E.;
"Crystal structure of chemically synthesized [N33A] stromal cell-
derived factor 1alpha, a potent ligand for the HIV-1 'fusin'
coreceptor.";
Proc. Natl. Acad. Sci. U.S.A. 95:6941-6946(1998).
[28]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-88, DISULFIDE BONDS, AND
MUTAGENESIS OF ARG-33; PHE-34; PHE-35; GLU-36; SER-37; HIS-38 AND
33-ARG--HIS-38.
PubMed=10954912; DOI=10.1089/10799900050116390;
Ohnishi Y., Senda T., Nandhagopal N., Sugimoto K., Shioda T.,
Nagal Y., Mitsui Y.;
"Crystal structure of recombinant native SDF-1alpha with additional
mutagenesis studies: an attempt at a more comprehensive interpretation
of accumulated structure-activity relationship data.";
J. Interferon Cytokine Res. 20:691-700(2000).
[29]
STRUCTURE BY NMR OF 22-89, AND DISULFIDE BONDS.
PubMed=15588815; DOI=10.1016/j.jmb.2004.11.003;
Gozansky E.K., Louis J.M., Caffrey M., Clore G.M.;
"Mapping the binding of the N-terminal extracellular tail of the CXCR4
receptor to stromal cell-derived factor-1alpha.";
J. Mol. Biol. 345:651-658(2005).
[30]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 22-88 IN COMPLEX WITH
HEPARIN DISACCHARIDE I-S, DISULFIDE BONDS, AND MUTAGENESIS OF ARG-29;
ARG-33; 34-PHE-PHE-35; 36-GLU--HIS-38; HIS-46; LYS-48; 52-THR--ALA-56;
ARG-62; ARG-68 AND GLN-69.
PubMed=17264079; DOI=10.1074/jbc.M608796200;
Murphy J.W., Cho Y., Sachpatzidis A., Fan C., Hodsdon M.E., Lolis E.;
"Structural and functional basis of CXCL12 (stromal cell-derived
factor-1 alpha) binding to heparin.";
J. Biol. Chem. 282:10018-10027(2007).
[31]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-89, DISULFIDE BONDS, AND
MUTAGENESIS OF LYS-22.
PubMed=17357154; DOI=10.1002/prot.21350;
Ryu E.K., Kim T.G., Kwon T.H., Jung I.D., Ryu D., Park Y.M., Kim J.,
Ahn K.H., Ban C.;
"Crystal structure of recombinant human stromal cell-derived factor-
1alpha.";
Proteins 67:1193-1197(2007).
[32]
STRUCTURE BY NMR OF 22-89 OF MUTANT CYS-57 AND CYS-86 IN COMPLEX WITH
CXCR4 FRAGMENT, SUBUNIT, DIMERIZATION, DISULFIDE BONDS, AND
MUTAGENESIS OF ARG-41; HIS-46; LYS-48; VAL-60; ARG-62; ARG-68; VAL-70;
GLU-81; GLU-84 AND LYS-85.
PubMed=18799424; DOI=10.1126/scisignal.1160755;
Veldkamp C.T., Seibert C., Peterson F.C., De la Cruz N.B.,
Haugner J.C. III, Basnet H., Sakmar T.P., Volkman B.F.;
"Structural basis of CXCR4 sulfotyrosine recognition by the chemokine
SDF-1/CXCL12.";
Sci. Signal. 1:RA4-RA4(2008).
[33]
STRUCTURE BY NMR OF 22-89, ASSAY ON RAT ISCHEMIA/REPERFUSION MODEL,
DIMERIZATION, AND DISULFIDE BONDS.
PubMed=19551879; DOI=10.1002/pro.167;
Veldkamp C.T., Ziarek J.J., Su J., Basnet H., Lennertz R.,
Weiner J.J., Peterson F.C., Baker J.E., Volkman B.F.;
"Monomeric structure of the cardioprotective chemokine SDF-1/CXCL12.";
Protein Sci. 18:1359-1369(2009).
[34]
STRUCTURE BY NMR OF 22-89, AND DISULFIDE BONDS.
Ziarek J.J., Veldkamp C.T., Peterson F.C., Volkman B.F.;
"Solution structure of human SDF1-alpha H25R.";
Submitted (SEP-2009) to the PDB data bank.
[35]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 22-88, AND DIMERIZATION.
PubMed=20077567; DOI=10.1002/prot.22666;
Murphy J.W., Yuan H., Kong Y., Xiong Y., Lolis E.J.;
"Heterologous quaternary structure of CXCL12 and its relationship to
the CC chemokine family.";
Proteins 78:1331-1337(2010).
-!- FUNCTION: Chemoattractant active on T-lymphocytes, monocytes, but
not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to
induce a rapid and transient rise in the level of intracellular
calcium ions and chemotaxis. Also binds to atypical chemokine
receptor ACKR3, which activates the beta-arrestin pathway and acts
as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1-
alpha(3-67) show a reduced chemotactic activity. Binding to cell
surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-
67) and thus to preserve activity on local sites. Acts as a
positive regulator of monocyte migration and a negative regulator
of monocyte adhesion via the LYN kinase. Stimulates migration of
monocytes and T-lymphocytes through its receptors, CXCR4 and
ACKR3, and decreases monocyte adherence to surfaces coated with
ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis
inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to
ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-
cell line-adapted HIV-1. Plays a protective role after myocardial
infarction. Induces down-regulation and internalization of ACKR3
expressed in various cells. Has several critical functions during
embryonic development; required for B-cell lymphopoiesis,
myelopoiesis in bone marrow and heart ventricular septum
formation. {ECO:0000269|PubMed:11069075,
ECO:0000269|PubMed:11859124, ECO:0000269|PubMed:16107333,
ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19255243,
ECO:0000269|PubMed:8752281}.
-!- SUBUNIT: Monomer or homodimer; in equilibrium. Dimer formation is
induced by non acidic pH and the presence of multivalent anions,
and by binding to CXCR4 or heparin. Monomeric form is required for
full chemotactic activity and resistance to ischemia/reperfusion
injury, whereas the dimeric form acts as a partial agonist of
CXCR4, stimulating Ca2+ mobilization but with no chemotactic
activity and instead acts as a selective antagonist that blocks
chemotaxis induced by the monomeric form. Interacts with the N-
terminus of ACKR3. {ECO:0000269|PubMed:10446158,
ECO:0000269|PubMed:16107333, ECO:0000269|PubMed:16725153,
ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424,
ECO:0000269|PubMed:19255243, ECO:0000269|PubMed:9427609}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=Beta; Synonyms=SDF-1-beta(1-72), hSDF-1beta;
IsoId=P48061-1; Sequence=Displayed;
Name=Alpha; Synonyms=SDF-1-alpha(1-68), hSDF-1alpha;
IsoId=P48061-2; Sequence=VSP_001056;
Name=Gamma; Synonyms=hSDF-1gamma, SDF-1g;
IsoId=P48061-3; Sequence=VSP_041209;
Name=Delta; Synonyms=hSDF-1delta;
IsoId=P48061-4; Sequence=VSP_042118;
Name=Epsilon; Synonyms=hSDFepsilon;
IsoId=P48061-5; Sequence=VSP_042119;
Name=Theta; Synonyms=hSDFphi, hSDFtheta, Phi;
IsoId=P48061-6; Sequence=VSP_042120;
Name=7;
IsoId=P48061-7; Sequence=VSP_054781;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Isoform Alpha and isoform Beta are
ubiquitously expressed, with highest levels detected in liver,
pancreas and spleen. Isoform Gamma is mainly expressed in heart,
with weak expression detected in several other tissues. Isoform
Delta, isoform Epsilon and isoform Theta have highest expression
levels in pancreas, with lower levels detected in heart, kidney,
liver and spleen. {ECO:0000269|PubMed:16626895}.
-!- DEVELOPMENTAL STAGE: Isoform Alpha is ubiquitously expressed in
fetal tissues. Isoform Beta and isoform Delta have more limited
expression patterns, with highest levels detected in fetal spleen
and fetal liver, respectively. Isoform Gamma and isoform Theta are
weakly detected in fetal kidney. {ECO:0000269|PubMed:16626895}.
-!- PTM: Processed forms SDF-1-beta(3-72) and SDF-1-alpha(3-67) are
produced after secretion by proteolytic cleavage of isoforms Beta
and Alpha, respectively. The N-terminal processing is probably
achieved by DPP4. Isoform Alpha is first cleaved at the C-terminus
to yield a SDF-1-alpha(1-67) intermediate before being processed
at the N-terminus. The C-terminal processing of isoform Alpha is
reduced by binding to heparin and, probably, cell surface
proteoglycans. {ECO:0000269|PubMed:14525775}.
-!- MASS SPECTROMETRY: Mass=7959; Method=Electrospray; Range=22-89
(P48061-2); Evidence={ECO:0000269|PubMed:14525775};
-!- MASS SPECTROMETRY: Mass=7606; Method=Electrospray; Range=24-88
(P48061-2); Evidence={ECO:0000269|PubMed:14525775};
-!- MASS SPECTROMETRY: Mass=8522; Method=Electrospray; Range=22-93
(P48061-1); Evidence={ECO:0000269|PubMed:14525775};
-!- MASS SPECTROMETRY: Mass=8297; Method=Electrospray; Range=24-93
(P48061-1); Evidence={ECO:0000269|PubMed:14525775};
-!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAC10202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=SDF-1 entry;
URL="https://en.wikipedia.org/wiki/SDF-1_%28biology%29";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cxcl12/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; L36033; AAB39332.1; -; mRNA.
EMBL; L36034; AAB39333.1; -; mRNA.
EMBL; DQ345517; ABC69270.1; -; mRNA.
EMBL; DQ345518; ABC69271.1; -; mRNA.
EMBL; DQ345519; ABC69272.1; -; mRNA.
EMBL; DQ345520; ABC69273.1; -; mRNA.
EMBL; U16752; AAA97434.1; -; mRNA.
EMBL; U19495; AAB40516.1; -; mRNA.
EMBL; AY644456; AAT76437.1; -; mRNA.
EMBL; AY874118; AAW82036.1; -; mRNA.
EMBL; CR450283; CAG29279.1; -; mRNA.
EMBL; AK292628; BAF85317.1; -; mRNA.
EMBL; AK311814; BAG34757.1; -; mRNA.
EMBL; AU120056; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY802782; AAV49999.1; -; Genomic_DNA.
EMBL; AL137026; CAC10202.1; ALT_SEQ; Genomic_DNA.
EMBL; AL137026; CAC10203.1; -; Genomic_DNA.
EMBL; CH471160; EAW86619.1; -; Genomic_DNA.
EMBL; BC039893; AAH39893.1; -; mRNA.
CCDS; CCDS31186.1; -. [P48061-3]
CCDS; CCDS44373.1; -. [P48061-1]
CCDS; CCDS53527.1; -. [P48061-4]
CCDS; CCDS60518.1; -. [P48061-7]
CCDS; CCDS7207.1; -. [P48061-2]
PIR; G01540; G01540.
RefSeq; NP_000600.1; NM_000609.6. [P48061-1]
RefSeq; NP_001029058.1; NM_001033886.2. [P48061-3]
RefSeq; NP_001171605.1; NM_001178134.1. [P48061-4]
RefSeq; NP_001264919.1; NM_001277990.1. [P48061-7]
RefSeq; NP_954637.1; NM_199168.3. [P48061-2]
UniGene; Hs.522891; -.
PDB; 1A15; X-ray; 2.20 A; A/B=22-88.
PDB; 1QG7; X-ray; 2.00 A; A/B=22-88.
PDB; 1SDF; NMR; -; A=22-88.
PDB; 1VMC; NMR; -; A=22-89.
PDB; 2J7Z; X-ray; 1.95 A; A/B=22-89.
PDB; 2K01; NMR; -; A/C=22-89.
PDB; 2K03; NMR; -; A/C=22-89.
PDB; 2K04; NMR; -; A/C=22-89.
PDB; 2K05; NMR; -; A/C=22-89.
PDB; 2KEC; NMR; -; A=22-89.
PDB; 2KED; NMR; -; A=22-89.
PDB; 2KEE; NMR; -; A=22-89.
PDB; 2KOL; NMR; -; A=22-89.
PDB; 2N55; NMR; -; A=22-89.
PDB; 2NWG; X-ray; 2.07 A; A/B=22-88.
PDB; 2SDF; NMR; -; A=22-88.
PDB; 3GV3; X-ray; 1.60 A; A=26-88.
PDB; 3HP3; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=22-88.
PDB; 4LMQ; X-ray; 2.77 A; D/F=29-89.
PDB; 4UAI; X-ray; 1.90 A; A/B=22-89.
PDBsum; 1A15; -.
PDBsum; 1QG7; -.
PDBsum; 1SDF; -.
PDBsum; 1VMC; -.
PDBsum; 2J7Z; -.
PDBsum; 2K01; -.
PDBsum; 2K03; -.
PDBsum; 2K04; -.
PDBsum; 2K05; -.
PDBsum; 2KEC; -.
PDBsum; 2KED; -.
PDBsum; 2KEE; -.
PDBsum; 2KOL; -.
PDBsum; 2N55; -.
PDBsum; 2NWG; -.
PDBsum; 2SDF; -.
PDBsum; 3GV3; -.
PDBsum; 3HP3; -.
PDBsum; 4LMQ; -.
PDBsum; 4UAI; -.
ProteinModelPortal; P48061; -.
SMR; P48061; -.
BioGrid; 112288; 6.
DIP; DIP-391N; -.
IntAct; P48061; 6.
MINT; MINT-6491347; -.
STRING; 9606.ENSP00000379140; -.
BindingDB; P48061; -.
ChEMBL; CHEMBL3286074; -.
DrugBank; DB06822; Tinzaparin.
iPTMnet; P48061; -.
PhosphoSitePlus; P48061; -.
BioMuta; CXCL12; -.
DMDM; 1352728; -.
PaxDb; P48061; -.
PeptideAtlas; P48061; -.
PRIDE; P48061; -.
Ensembl; ENST00000343575; ENSP00000339913; ENSG00000107562. [P48061-2]
Ensembl; ENST00000374426; ENSP00000363548; ENSG00000107562. [P48061-3]
Ensembl; ENST00000374429; ENSP00000363551; ENSG00000107562. [P48061-1]
Ensembl; ENST00000395793; ENSP00000379139; ENSG00000107562. [P48061-7]
Ensembl; ENST00000395794; ENSP00000379140; ENSG00000107562. [P48061-4]
Ensembl; ENST00000395795; ENSP00000379141; ENSG00000107562. [P48061-7]
GeneID; 6387; -.
KEGG; hsa:6387; -.
UCSC; uc001jbf.5; human. [P48061-1]
CTD; 6387; -.
DisGeNET; 6387; -.
EuPathDB; HostDB:ENSG00000107562.16; -.
GeneCards; CXCL12; -.
H-InvDB; HIX0008784; -.
HGNC; HGNC:10672; CXCL12.
HPA; CAB017564; -.
MalaCards; CXCL12; -.
MIM; 600835; gene.
neXtProt; NX_P48061; -.
OpenTargets; ENSG00000107562; -.
PharmGKB; PA35602; -.
eggNOG; ENOG410J1S5; Eukaryota.
eggNOG; ENOG4112BS6; LUCA.
GeneTree; ENSGT00390000014056; -.
HOGENOM; HOG000220915; -.
HOVERGEN; HBG107437; -.
InParanoid; P48061; -.
KO; K10031; -.
OMA; STPNCAL; -.
OrthoDB; EOG091G14JB; -.
PhylomeDB; P48061; -.
TreeFam; TF353159; -.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-376176; Signaling by ROBO receptors.
Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SIGNOR; P48061; -.
ChiTaRS; CXCL12; human.
EvolutionaryTrace; P48061; -.
GeneWiki; Stromal_cell-derived_factor-1; -.
GenomeRNAi; 6387; -.
PMAP-CutDB; Q5IT36; -.
PRO; PR:P48061; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107562; -.
CleanEx; HS_CXCL12; -.
Genevisible; P48061; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
GO; GO:0042379; F:chemokine receptor binding; IMP:UniProtKB.
GO; GO:0045236; F:CXCR chemokine receptor binding; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:0008015; P:blood circulation; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:ProtInc.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0006935; P:chemotaxis; TAS:UniProtKB.
GO; GO:0006952; P:defense response; IEA:InterPro.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IDA:BHF-UCL.
GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; IDA:BHF-UCL.
GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; IDA:UniProtKB.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IEA:Ensembl.
GO; GO:0090280; P:positive regulation of calcium ion import; TAS:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:MGI.
GO; GO:0033603; P:positive regulation of dopamine secretion; IEA:Ensembl.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
GO; GO:2000406; P:positive regulation of T cell migration; IDA:MGI.
GO; GO:0008064; P:regulation of actin polymerization or depolymerization; TAS:ProtInc.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:1990478; P:response to ultrasound; IEA:Ensembl.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0010818; P:T cell chemotaxis; IDA:UniProtKB.
GO; GO:0022029; P:telencephalon cell migration; IEA:Ensembl.
CDD; cd00273; Chemokine_CXC; 1.
InterPro; IPR001811; Chemokine_IL8-like_dom.
InterPro; IPR033899; CXC_Chemokine_domain.
InterPro; IPR036048; Interleukin_8-like_sf.
Pfam; PF00048; IL8; 1.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chemotaxis; Complete proteome;
Cytokine; Disulfide bond; Growth factor; Reference proteome; Secreted;
Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 93 Stromal cell-derived factor 1.
/FTId=PRO_0000005109.
CHAIN 24 93 SDF-1-beta(3-72).
/FTId=PRO_0000005110.
CHAIN 24 88 SDF-1-alpha(3-67).
/FTId=PRO_0000005111.
REGION 29 33 Receptor and heparin binding.
{ECO:0000305}.
REGION 39 41 Receptor binding.
REGION 41 51 Heparin binding.
REGION 48 50 Receptor binding.
REGION 60 70 Receptor binding.
MOTIF 22 23 Receptor activation motif.
BINDING 62 62 Heparin.
BINDING 69 69 Heparin.
BINDING 85 85 Heparin.
SITE 46 46 Important for dimer formation.
DISULFID 30 55
DISULFID 32 71
VAR_SEQ 39 93 VARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWI
QEYLEKALNKRFKM -> YCTCLIRVSFHGATPLTQGSWVL
YSLSCAGGETGLREPGPMVSPRVESHQEGRLGVPGPVNLGK
A (in isoform 7).
{ECO:0000303|PubMed:16344560}.
/FTId=VSP_054781.
VAR_SEQ 89 93 KRFKM -> NLISAAPAGKRVIAGARALHPSPPRACPTARA
LCEIRLWPPPEWSWPSPGDV (in isoform Delta).
{ECO:0000303|PubMed:16626895}.
/FTId=VSP_042118.
VAR_SEQ 89 93 KRFKM -> NC (in isoform Epsilon).
{ECO:0000303|PubMed:16626895}.
/FTId=VSP_042119.
VAR_SEQ 90 93 Missing (in isoform Alpha).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7490086,
ECO:0000303|Ref.4, ECO:0000303|Ref.6,
ECO:0000303|Ref.7}.
/FTId=VSP_001056.
VAR_SEQ 90 93 RFKM -> GRREEKVGKKEKIGKKKRQKKRKAAQKRKN
(in isoform Gamma).
{ECO:0000303|PubMed:16626895,
ECO:0000303|Ref.5}.
/FTId=VSP_041209.
VAR_SEQ 90 93 RFKM -> IWLYGNAETSR (in isoform Theta).
{ECO:0000303|PubMed:16626895}.
/FTId=VSP_042120.
MUTAGEN 22 23 Missing: Abolished CXCR4 activation
ability, but only slightly impaired
binding to the receptor.
{ECO:0000269|PubMed:9384579}.
MUTAGEN 22 22 K->A: Loss of chemotactic activity.
{ECO:0000269|PubMed:17357154,
ECO:0000269|PubMed:9384579}.
MUTAGEN 22 22 K->R: Abolished CXCR4 activation ability,
but only slightly impaired binding to the
receptor. {ECO:0000269|PubMed:17357154,
ECO:0000269|PubMed:9384579}.
MUTAGEN 22 22 Missing: Abolished CXCR4 activation
ability, but only slightly impaired
binding to the receptor.
{ECO:0000269|PubMed:17357154,
ECO:0000269|PubMed:9384579}.
MUTAGEN 23 23 P->G: Abolished CXCR4 activation ability,
but only slightly impaired binding to the
receptor. {ECO:0000269|PubMed:9384579}.
MUTAGEN 25 27 SLS->AQA: Significantly impaired CXCR4
activation ability, but only slightly
impaired binding to the receptor.
{ECO:0000269|PubMed:9384579}.
MUTAGEN 28 28 Y->A: Impaired CXCR4 activation ability,
but only slightly impaired binding to the
receptor. {ECO:0000269|PubMed:9384579}.
MUTAGEN 28 28 Y->H: No significant effect on CXCR4
binding or activation.
{ECO:0000269|PubMed:9384579}.
MUTAGEN 29 29 R->K: Slightly impaired binding and
activation of CXCR4.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:9384579}.
MUTAGEN 29 29 R->Q: Greatly impaired chemotactic
activity and enhanced inhibition by
heparin. {ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:9384579}.
MUTAGEN 33 38 RFFESH->AAAAAA: Significantly decreased
chemotactic activity.
{ECO:0000269|PubMed:10954912}.
MUTAGEN 33 33 R->A: Significantly decreased anti-HIV-1
and chemotactic activities.
{ECO:0000269|PubMed:10954912,
ECO:0000269|PubMed:17264079}.
MUTAGEN 33 33 R->Q: Slightly impaired chemotactic
activity and enhanced inhibition by
heparin. Greatly impaired chemotactic
activity; when associated with Q-29.
{ECO:0000269|PubMed:10954912,
ECO:0000269|PubMed:17264079}.
MUTAGEN 34 34 F->A: No effect on anti-HIV-1 and
chemotactic activities. Slightly impaired
chemotactic activity and no effect on
inhibition by heparin; when associated
with A-35. {ECO:0000269|PubMed:10954912}.
MUTAGEN 35 35 F->A: No effect on anti-HIV-1 and
chemotactic activities. Slightly impaired
chemotactic activity and no effect on
inhibition by heparin; when associated
with A-34. {ECO:0000269|PubMed:10954912}.
MUTAGEN 36 38 ESH->QSN: Slightly impaired chemotactic
activity, no effect on inhibition by
heparin. {ECO:0000269|PubMed:17264079}.
MUTAGEN 36 36 E->A: No effect on anti-HIV-1 and
chemotactic activities.
{ECO:0000269|PubMed:10954912}.
MUTAGEN 37 37 S->A: No effect on anti-HIV-1 and
chemotactic activities.
{ECO:0000269|PubMed:10954912}.
MUTAGEN 38 38 H->A: No effect on anti-HIV-1 and
chemotactic activities.
{ECO:0000269|PubMed:10954912}.
MUTAGEN 41 41 R->A: No effect on CXCR4 activation.
{ECO:0000269|PubMed:18799424}.
MUTAGEN 45 48 KHLK->SSLS: Loss of heparin-binding
capacity. {ECO:0000269|PubMed:10446158}.
MUTAGEN 46 46 H->A: Reduced dimerization in neutral pH.
Eliminates the pH dependence of
dimerization.
{ECO:0000269|PubMed:15741341,
ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 46 46 H->L: No significant effect on
dimerization in neutral pH. Eliminates
the pH dependence of dimerization.
{ECO:0000269|PubMed:15741341,
ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 46 46 H->N: Slightly impaired CXCR4 activation
and clear resistance to inhibition by
heparin; when associated with Q-48; Q-62;
Q-68 and N-69.
{ECO:0000269|PubMed:15741341,
ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 46 46 H->R: No effect on CXCR4 activation.
Impaired dimer formation, leading to
increased chemotactic activity.
Eliminates the pH dependence of
dimerization.
{ECO:0000269|PubMed:15741341,
ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 48 48 K->A: Impaired CXCR4 activation.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 48 48 K->E: Impaired CXCR4 activation.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 48 48 K->Q: Slightly impaired CXCR4 activation
and clear resistance to inhibition by
heparin; when associated with N-46; Q-62;
Q-68 and N-69.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 52 56 TPNCA->GPGCG: Slightly impaired
chemotactic activity, no effect on
inhibition by heparin.
{ECO:0000269|PubMed:17264079}.
MUTAGEN 57 57 L->C: Formation of an intermolecular
disulfide bond, leading to a locked
dimer; when associated with C-86. No
effect on CXCR4 activation, but loss of
chemotactic activity; when associated
with C-86.
MUTAGEN 60 60 V->A: Impaired CXCR4 activation.
{ECO:0000269|PubMed:18799424}.
MUTAGEN 62 62 R->A: No effect on CXCR4 activation.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 62 62 R->Q: Slightly impaired CXCR4 activation
and clear resistance to inhibition by
heparin; when associated with N-46; Q-48;
Q-68 and N-69.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 68 68 R->A: Impaired CXCR4 activation.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 68 68 R->E: Greatly impaired CXCR4 activation.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 68 68 R->Q: Slightly impaired CXCR4 activation
and clear resistance to inhibition by
heparin; when associated with N-46; Q-48;
Q-62 and N-69.
{ECO:0000269|PubMed:17264079,
ECO:0000269|PubMed:18799424}.
MUTAGEN 69 69 Q->N: Slightly impaired CXCR4 activation
and clear resistance to inhibition by
heparin; when associated with N-46; Q-48;
Q-62 and Q-68.
{ECO:0000269|PubMed:17264079}.
MUTAGEN 70 70 V->A: Impaired CXCR4 activation.
{ECO:0000269|PubMed:18799424}.
MUTAGEN 81 81 E->A: No effect on CXCR4 activation.
{ECO:0000269|PubMed:18799424}.
MUTAGEN 84 84 E->A: No effect on CXCR4 activation.
{ECO:0000269|PubMed:18799424}.
MUTAGEN 85 85 K->A: No effect on CXCR4 activation.
{ECO:0000269|PubMed:18799424}.
MUTAGEN 86 86 A->C: Formation of an intermolecular
disulfide bond, leading to a locked
dimer; when associated with C-57. No
effect on CXCR4 activation, but loss of
chemotactic activity; when associated
with C-57.
HELIX 24 26 {ECO:0000244|PDB:4UAI}.
STRAND 27 29 {ECO:0000244|PDB:2K01}.
STRAND 31 34 {ECO:0000244|PDB:3HP3}.
STRAND 36 38 {ECO:0000244|PDB:1VMC}.
HELIX 41 43 {ECO:0000244|PDB:3GV3}.
STRAND 44 49 {ECO:0000244|PDB:3GV3}.
TURN 53 55 {ECO:0000244|PDB:1QG7}.
STRAND 59 63 {ECO:0000244|PDB:3GV3}.
TURN 64 66 {ECO:0000244|PDB:3GV3}.
STRAND 69 72 {ECO:0000244|PDB:3GV3}.
HELIX 79 86 {ECO:0000244|PDB:3GV3}.
SEQUENCE 93 AA; 10666 MW; 505B5A29C2B44E8D CRC64;
MNAKVVVVLV LVLTALCLSD GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV
ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM


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E0477h ELISA C-X-C motif chemokine 12,CXCL12,hIRH,Homo sapiens,hSDF-1,Human,Intercrine reduced in hepatomas,IRH,PBSF,Pre-B cell growth-stimulating factor,SDF1,SDF-1,SDF1A,SDF1B,Stromal cell-derived factor 1 96T
E0477h ELISA kit C-X-C motif chemokine 12,CXCL12,hIRH,Homo sapiens,hSDF-1,Human,Intercrine reduced in hepatomas,IRH,PBSF,Pre-B cell growth-stimulating factor,SDF1,SDF-1,SDF1A,SDF1B,Stromal cell-derived fact 96T
10-663-45032 Stromal Cell-Derived Factor-1 beta (CXCL12) Murine - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 0.002 mg
10-663-45032 Stromal Cell-Derived Factor-1 beta (CXCL12) Murine - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 1 mg
10-663-45032 Stromal Cell-Derived Factor-1 beta (CXCL12) Murine - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 0.01 mg
10-663-45009 Stromal Cell-Derived Factor-1 alpha (SDF-1. CXCL12) Human - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 0.002 mg
10-663-45030 Stromal Cell-Derived Factor-1 alpha (CXCL12) Murine - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 0.002 mg
10-663-45009 Stromal Cell-Derived Factor-1 alpha (SDF-1. CXCL12) Human - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 1 mg
10-663-45009 Stromal Cell-Derived Factor-1 alpha (SDF-1. CXCL12) Human - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 0.01 mg
10-663-45030 Stromal Cell-Derived Factor-1 alpha (CXCL12) Murine - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 0.01 mg
10-663-45030 Stromal Cell-Derived Factor-1 alpha (CXCL12) Murine - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH N_A 1 mg
18-003-42912 Stromal cell-derived factor 1 - SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH Polyclonal 0.05 mg Aff Pur
E0477m ELISA 12-O-tetradecanoylphorbol 13-acetate repressed protein 1,C-X-C motif chemokine 12,Cxcl12,Mouse,Mus musculus,PBSF,Pre-B cell growth-stimulating factor,Sdf1,SDF-1,Stromal cell-derived factor 1,Thy 96T
E0477m ELISA kit 12-O-tetradecanoylphorbol 13-acetate repressed protein 1,C-X-C motif chemokine 12,Cxcl12,Mouse,Mus musculus,PBSF,Pre-B cell growth-stimulating factor,Sdf1,SDF-1,Stromal cell-derived factor 96T
U0477m CLIA 12-O-tetradecanoylphorbol 13-acetate repressed protein 1,C-X-C motif chemokine 12,Cxcl12,Mouse,Mus musculus,PBSF,Pre-B cell growth-stimulating factor,Sdf1,SDF-1,Stromal cell-derived factor 1,Thym 96T
18-783-75593 GOAT ANTI HUMAN SDF-1 BETA - CXCL12b; SDF-1; C-X-C motif chemokine 12; Pre-B cell growth-stimulating factor; PBSF; hIRH Polyclonal 0.1 mg
18-783-75653 RABBIT ANTI HUMAN SDF-1 ALPHA - CXCL12a; SDF-1; C-X-C motif chemokine 12; Pre-B cell growth-stimulating factor; PBSF; hIRH Polyclonal 0.1 mg
18-783-78903 GOAT ANTI HUMAN SDF-1 BETA Biotin - CXCL12b; SDF-1; C-X-C motif chemokine 12; Pre-B cell growth-stimulating factor; PBSF; hIRH Polyclonal 0.05 mg
18-783-78928 RABBIT ANTI HUMAN SDF-1 ALPHA Biotin - CXCL12a; SDF-1; C-X-C motif chemokine 12; Pre-B cell growth-stimulating factor; PBSF; hIRH Polyclonal 0.05 mg
RD172175100 Stromal cell_derived factor 1, isoform alpha (SDF_1a, C_X_C motif chemokine 12, Pre_B cell growth_stimulating factor, PBSF, hIRH, CXCL12) 0.1 mg
18-272-195073 SDF1 - Goat polyclonal to SDF1; SDF-1; CXCL12; Pre-B cell growth-stimulating factor; PBSF; hIRH Polyclonal 0.025 mg
GWB-118726 CXCL12 (chemokine (C-X-C motif) ligand 12 (stromal cell-derived factor 1))
orb82157 Stromal Cell-Derived Factor-1a, recombinant protein Stromal Cell Derived Factor 1 alpha (SDF-1a) 8kDa, Recombinant is a purified cytokine_growth factor. For research use only. 10
31-056 Stromal cell-derived factors 1-alpha and 1-beta are small cytokines that belong to the intercrine family, members of which activate leukocytes and are often induced by proinflammatory stimuli such as 0.05 mg


 

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