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Interleukin-8 (IL-8) (C-X-C motif chemokine 8) (Chemokine (C-X-C motif) ligand 8) (Emoctakin) (Granulocyte chemotactic protein 1) (GCP-1) (Monocyte-derived neutrophil chemotactic factor) (MDNCF) (Monocyte-derived neutrophil-activating peptide) (MONAP) (Neutrophil-activating protein 1) (NAP-1) (Protein 3-10C) (T-cell chemotactic factor) [Cleaved into: MDNCF-a (GCP/IL-8 protein IV) (IL8/NAP1 form I); Interleukin-8 ((Ala-IL-8)77) (GCP/IL-8 protein II) (IL-8(1-77)) (IL8/NAP1 form II) (MDNCF-b); IL-8(5-77); IL-8(6-77) ((Ser-IL-8)72) (GCP/IL-8 protein I) (IL8/NAP1 form III) (Lymphocyte-derived neutrophil-activating factor) (LYNAP) (MDNCF-c) (Neutrophil-activating factor) (NAF); IL-8(7-77) (GCP/IL-8 protein V) (IL8/NAP1 form IV); IL-8(8-77) (GCP/IL-8 protein VI) (IL8/NAP1 form V); IL-8(9-77) (GCP/IL-8 protein III) (IL8/NAP1 form VI)]

 IL8_HUMAN               Reviewed;          99 AA.
P10145; B2R4L8; Q6FGF6; Q6LAE6; Q96RG6; Q9C077; Q9UCE1; Q9UCR8;
Q9UCR9; Q9UCS0;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
16-OCT-2019, entry version 222.
RecName: Full=Interleukin-8;
Short=IL-8;
AltName: Full=C-X-C motif chemokine 8;
AltName: Full=Chemokine (C-X-C motif) ligand 8;
AltName: Full=Emoctakin;
AltName: Full=Granulocyte chemotactic protein 1;
Short=GCP-1;
AltName: Full=Monocyte-derived neutrophil chemotactic factor;
Short=MDNCF;
AltName: Full=Monocyte-derived neutrophil-activating peptide;
Short=MONAP;
AltName: Full=Neutrophil-activating protein 1;
Short=NAP-1;
AltName: Full=Protein 3-10C;
AltName: Full=T-cell chemotactic factor;
Contains:
RecName: Full=MDNCF-a;
AltName: Full=GCP/IL-8 protein IV;
AltName: Full=IL8/NAP1 form I;
Contains:
RecName: Full=Interleukin-8;
AltName: Full=(Ala-IL-8)77;
AltName: Full=GCP/IL-8 protein II;
AltName: Full=IL-8(1-77);
AltName: Full=IL8/NAP1 form II;
AltName: Full=MDNCF-b;
Contains:
RecName: Full=IL-8(5-77);
Contains:
RecName: Full=IL-8(6-77);
AltName: Full=(Ser-IL-8)72;
AltName: Full=GCP/IL-8 protein I;
AltName: Full=IL8/NAP1 form III;
AltName: Full=Lymphocyte-derived neutrophil-activating factor;
Short=LYNAP;
AltName: Full=MDNCF-c;
AltName: Full=Neutrophil-activating factor;
Short=NAF;
Contains:
RecName: Full=IL-8(7-77);
AltName: Full=GCP/IL-8 protein V;
AltName: Full=IL8/NAP1 form IV;
Contains:
RecName: Full=IL-8(8-77);
AltName: Full=GCP/IL-8 protein VI;
AltName: Full=IL8/NAP1 form V;
Contains:
RecName: Full=IL-8(9-77);
AltName: Full=GCP/IL-8 protein III;
AltName: Full=IL8/NAP1 form VI;
Flags: Precursor;
Name=CXCL8; Synonyms=IL8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2953813;
Schmid J., Weissmann C.;
"Induction of mRNA for a serine protease and a beta-thromboglobulin-
like protein in mitogen-stimulated human leukocytes.";
J. Immunol. 139:250-256(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3260265; DOI=10.1084/jem.167.6.1883;
Matsushima K., Morishita K., Yoshimura T., Lavu S., Kobayashi Y.,
Lew W., Appella E., Kung H., Leonard E.J., Oppenheim J.J.;
"Molecular cloning of a human monocyte-derived neutrophil chemotactic
factor (MDNCF) and the induction of MDNCF mRNA by interleukin 1 and
tumor necrosis factor.";
J. Exp. Med. 167:1883-1893(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2663993;
Mukaida N., Shiroo M., Matsushima K.;
"Genomic structure of the human monocyte-derived neutrophil
chemotactic factor IL-8.";
J. Immunol. 143:1366-1371(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2664463; DOI=10.1128/mcb.9.5.1946;
Kowalski J., Denhardt D.T.;
"Regulation of the mRNA for monocyte-derived neutrophil-activating
peptide in differentiating HL60 promyelocytes.";
Mol. Cell. Biol. 9:1946-1957(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lung carcinoma;
PubMed=2200751; DOI=10.1016/0165-2478(90)90043-p;
Hotta K., Hayashi K., Ishikawa J., Tagawa M., Hashimoto K., Mizuno S.,
Suzuki K.;
"Coding region structure of interleukin-8 gene of human lung giant
cell carcinoma LU65C cells that produce LUCT/interleukin-8:
homogeneity in interleukin-8 genes.";
Immunol. Lett. 24:165-169(1990).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Neutrophil;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[10]
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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-91.
TISSUE=Peripheral blood leukocyte;
Jang J.S., Kim B.E.;
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-97.
TISSUE=Kidney;
King C.H., Gordon G.S., Konieczkowski M., Sedor J.R.;
"cDNA cloning of human mesangial cell interleukin 8 by polymerase
chain reaction.";
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
[14]
PROTEIN SEQUENCE OF 21-41, IDENTIFICATION OF MDNCF-A; IL-8(1-77);
IL-8(6-77); IL-8(7-77); IL-8(8-77) AND IL-8(9-77), AND PROTEOLYTIC
PROCESSING OF N-TERMINUS.
PubMed=2523801; DOI=10.1111/j.1432-1033.1989.tb14729.x;
van Damme J., van Beeumen J., Conings R., Decock B., Billiau A.;
"Purification of granulocyte chemotactic peptide/interleukin-8 reveals
N-terminal sequence heterogeneity similar to that of beta-
thromboglobulin.";
Eur. J. Biochem. 181:337-344(1989).
[15]
PROTEIN SEQUENCE OF 21-41, IDENTIFICATION OF MDNCF-A; IL-8(1-77);
IL-8(6-77); IL-8(7-77); IL-8(8-77) AND IL-8(9-77), PROTEOLYTIC
PROCESSING OF N-TERMINUS, AND FUNCTION.
PubMed=2145175; DOI=10.1002/eji.1830200933;
van Damme J., Rampart M., Coning R., Decock B., van Osselaer N.,
Willems J., Billiau A.;
"The neutrophil-activating proteins interleukin 8 and beta-
thromboglobulin: in vitro and in vivo comparison of NH2-terminally
processed forms.";
Eur. J. Immunol. 20:2113-2118(1990).
[16]
PROTEIN SEQUENCE OF 21-32, IDENTIFICATION OF MDNCF-A; IL-8(1-77) AND
IL-8(6-77), AND PROTEOLYTIC PROCESSING OF N-TERMINUS.
PubMed=2648135; DOI=10.1016/0161-5890(89)90024-2;
Yoshimura T., Robinson E.A., Appella E., Matsushima K.,
Showalter S.D., Skeel A., Leonard E.J.;
"Three forms of monocyte-derived neutrophil chemotactic factor (MDNCF)
distinguished by different lengths of the amino-terminal sequence.";
Mol. Immunol. 26:87-93(1989).
[17]
PROTEIN SEQUENCE OF 23-54, AND IDENTIFICATION OF IL-8(1-77).
PubMed=2659722; DOI=10.1084/jem.169.6.1895;
Suzuki K., Miyasaka H., Ota H., Yamakawa Y., Tagawa M., Kuramoto A.,
Mizuno S.;
"Purification and partial primary sequence of a chemotactic protein
for polymorphonuclear leukocytes derived from human lung giant cell
carcinoma LU65C cells.";
J. Exp. Med. 169:1895-1901(1989).
[18]
PROTEIN SEQUENCE OF 23-47.
TISSUE=Skin;
PubMed=1755384; DOI=10.1007/978-1-4684-6009-4_12;
Schroeder J.-M.;
"Biochemical and biological characterization of NAP-1/IL-8-related
cytokines in lesional psoriatic scale.";
Adv. Exp. Med. Biol. 305:97-107(1991).
[19]
PROTEIN SEQUENCE OF 23-46, AND IDENTIFICATION OF IL-8(1-77).
PubMed=2655583; DOI=10.1042/bj2590585;
Golds E.E., Mason P., Nyirkos P.;
"Inflammatory cytokines induce synthesis and secretion of gro protein
and a neutrophil chemotactic factor but not beta 2-microglobulin in
human synovial cells and fibroblasts.";
Biochem. J. 259:585-588(1989).
[20]
PROTEIN SEQUENCE OF 23-42.
TISSUE=Chronic myeloid leukemia cell;
PubMed=8344717; DOI=10.1016/0165-2478(93)90071-9;
Suzuki K., Yamakawa Y., Matsuo Y., Kamiya T., Minowada J., Mizuno S.;
"Isolation and amino acid sequence of a chemotactic protein,
LECT/interleukin 8, from a human myeloid leukemia cell line, ML-1.";
Immunol. Lett. 36:71-81(1993).
[21]
PROTEIN SEQUENCE OF 28-99, AND IDENTIFICATION OF IL-8(6-77).
PubMed=3279957; DOI=10.1016/s0006-291x(88)80364-4;
Gregory H., Young J., Schroeder J.-M., Mrowietz U., Christophers E.;
"Structure determination of a human lymphocyte derived neutrophil
activating peptide (LYNAP).";
Biochem. Biophys. Res. Commun. 151:883-890(1988).
[22]
PROTEIN SEQUENCE OF 28-69, AND IDENTIFICATION OF IL-8(6-77).
PubMed=3480540; DOI=10.1073/pnas.84.24.9233;
Yoshimura T., Matsushima K., Tanaka S., Robinson E.A., Appella E.,
Oppenheim J.J., Leonard E.J.;
"Purification of a human monocyte-derived neutrophil chemotactic
factor that has peptide sequence similarity to other host defense
cytokines.";
Proc. Natl. Acad. Sci. U.S.A. 84:9233-9237(1987).
[23]
PROTEIN SEQUENCE OF 28-59, AND IDENTIFICATION OF IL-8(6-77).
PubMed=3322281; DOI=10.1016/0006-291x(87)90432-3;
Walz A., Peveri P., Aschauer H., Baggiolini M.;
"Purification and amino acid sequencing of NAF, a novel neutrophil-
activating factor produced by monocytes.";
Biochem. Biophys. Res. Commun. 149:755-761(1987).
[24]
PROTEOLYTIC PROCESSING OF N-TERMINUS BY THROMBIN, AND FUNCTION.
PubMed=2212672;
Hebert C.A., Luscinskas F.W., Kiely J.-M., Luis E.A., Darbonne W.C.,
Bennett G.L., Liu C.C., Obin M.S., Gimbrone M.A. Jr., Baker J.B.;
"Endothelial and leukocyte forms of IL-8. Conversion by thrombin and
interactions with neutrophils.";
J. Immunol. 145:3033-3040(1990).
[25]
SYNTHESIS OF 28-99.
PubMed=2007144; DOI=10.1021/bi00226a021;
Clark-Lewis I., Mose B., Walz A., Baggiolini M., Scott G.J.,
Aebersold R.;
"Chemical synthesis, purification, and characterization of two
inflammatory proteins, neutrophil activating peptide 1 (interleukin-8)
and neutrophil activating peptide.";
Biochemistry 30:3128-3135(1991).
[26]
PROTEOLYTIC PROCESSING OF N-TERMINUS BY MMP9.
PubMed=11023497;
Van den Steen P.E., Proost P., Wuyts A., Van Damme J., Opdenakker G.;
"Neutrophil gelatinase B potentiates interleukin-8 tenfold by
aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-
alpha and leaves RANTES and MCP-2 intact.";
Blood 96:2673-2681(2000).
[27]
IDENTIFICATION OF IL-8(5-77) AND IL-8(6-77), FUNCTION, AND PROTEOLYTIC
PROCESSING OF N-TERMINUS.
PubMed=11978786; DOI=10.1074/jbc.m112275200;
Schutyser E., Struyf S., Proost P., Opdenakker G., Laureys G.,
Verhasselt B., Peperstraete L., Van de Putte I., Saccani A.,
Allavena P., Mantovani A., Van Damme J.;
"Identification of biologically active chemokine isoforms from ascitic
fluid and elevated levels of CCL18/pulmonary and activation-regulated
chemokine in ovarian carcinoma.";
J. Biol. Chem. 277:24584-24593(2002).
[28]
REVIEW.
PubMed=1639201; DOI=10.1016/0014-5793(92)80909-z;
Baggiolini M., Clark-Lewis I.;
"Interleukin-8, a chemotactic and inflammatory cytokine.";
FEBS Lett. 307:97-101(1992).
[29]
REVIEW.
PubMed=14711052; DOI=10.1016/s0065-2776(03)81001-5;
Struyf S., Proost P., Van Damme J.;
"Regulation of the immune response by the interaction of chemokines
and proteases.";
Adv. Immunol. 81:1-44(2003).
[30]
CITRULLINATION AT ARG-27.
PubMed=18710930; DOI=10.1084/jem.20080305;
Proost P., Loos T., Mortier A., Schutyser E., Gouwy M., Noppen S.,
Dillen C., Ronsse I., Conings R., Struyf S., Opdenakker G.,
Maudgal P.C., Van Damme J.;
"Citrullination of CXCL8 by peptidylarginine deiminase alters receptor
usage, prevents proteolysis, and dampens tissue inflammation.";
J. Exp. Med. 205:2085-2097(2008).
[31]
CITRULLINATION AT ARG-27.
PubMed=19608678; DOI=10.3324/haematol.2009.006973;
Loos T., Opdenakker G., Van Damme J., Proost P.;
"Citrullination of CXCL8 increases this chemokine's ability to
mobilize neutrophils into the blood circulation.";
Haematologica 94:1346-1353(2009).
[32]
INDUCTION.
PubMed=20829347; DOI=10.1074/jbc.m110.136259;
Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.;
"Endoplasmic reticulum stress-activated C/EBP homologous protein
enhances nuclear factor-kappaB signals via repression of peroxisome
proliferator-activated receptor gamma.";
J. Biol. Chem. 285:35330-35339(2010).
[33]
STRUCTURE BY NMR OF 28-99.
PubMed=2681204;
Clore G.M., Appella E., Yamada M., Matsushima K., Gronenborn A.M.;
"Determination of the secondary structure of interleukin-8 by nuclear
magnetic resonance spectroscopy.";
J. Biol. Chem. 264:18907-18911(1989).
[34]
STRUCTURE BY NMR.
PubMed=2184886; DOI=10.1021/bi00459a004;
Clore G.M., Appella E., Yamada M., Matsushima K., Gronenborn A.M.;
"Three-dimensional structure of interleukin 8 in solution.";
Biochemistry 29:1689-1696(1990).
[35]
STRUCTURE BY NMR OF 28-80.
PubMed=8631339; DOI=10.1111/j.1432-1033.1996.00026.x;
Sticht H., Auer M., Schmitt B., Besemer J., Horcher M., Kirsch T.,
Lindley I.J., Rosch P.;
"Structure and activity of a chimeric interleukin-8-melanoma-growth-
stimulatory-activity protein.";
Eur. J. Biochem. 235:26-35(1996).
[36]
STRUCTURE BY NMR OF COMPLEX TO RECEPTOR.
PubMed=10368283; DOI=10.1016/s0969-2126(99)80022-7;
Skelton N.J., Quan C., Reilly D., Lowman H.;
"Structure of a CXC chemokine-receptor fragment in complex with
interleukin-8.";
Structure 7:157-168(1999).
[37]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=2182630;
Baldwin E.T., Franklin K.A., Appella E., Yamada M., Matsushima K.,
Wlodawer A., Weber I.T.;
"Crystallization of human interleukin-8. A protein chemotactic for
neutrophils and T-lymphocytes.";
J. Biol. Chem. 265:6851-6853(1990).
[38]
STRUCTURE BY NMR, AND COMPARISON WITH X-RAY STRUCTURE.
PubMed=2005614; DOI=10.1016/0022-2836(91)90518-b;
Clore G.M., Gronenborn A.M.;
"Comparison of the solution nuclear magnetic resonance and crystal
structures of interleukin-8. Possible implications for the mechanism
of receptor binding.";
J. Mol. Biol. 217:611-620(1991).
[39]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND STRUCTURE BY NMR.
PubMed=1988949; DOI=10.1073/pnas.88.2.502;
Baldwin E.T., Weber I.T., St Charles R., Xuan J.C., Appella E.,
Yamada M., Matsushima K., Edwards B.F., Clore G.M., Gronenborn A.M.;
"Crystal structure of interleukin 8: symbiosis of NMR and
crystallography.";
Proc. Natl. Acad. Sci. U.S.A. 88:502-506(1991).
[40]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANT.
PubMed=10707023;
DOI=10.1002/(sici)1097-0134(20000301)38:4<361::aid-prot2>3.0.co;2-0;
Gerber N., Lowman H., Artis D.R., Eigenbrot C.;
"Receptor-binding conformation of the 'ELR' motif of IL-8: X-ray
structure of the L5C/H33C variant at 2.35 A resolution.";
Proteins 38:361-367(2000).
-!- FUNCTION: IL-8 is a chemotactic factor that attracts neutrophils,
basophils, and T-cells, but not monocytes. It is also involved in
neutrophil activation. It is released from several cell types in
response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold
higher activity on neutrophil activation, IL-8(5-77) has increased
activity on neutrophil activation and IL-8(7-77) has a higher
affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77),
respectively. {ECO:0000269|PubMed:11978786,
ECO:0000269|PubMed:2145175, ECO:0000269|PubMed:2212672}.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P9WGV3:ahcY (xeno); NbExp=3; IntAct=EBI-3917999, EBI-11740468;
P25025:CXCR2; NbExp=3; IntAct=EBI-3917999, EBI-2835281;
P9WMN3:glmU (xeno); NbExp=3; IntAct=EBI-3917999, EBI-11740532;
P02776:PF4; NbExp=2; IntAct=EBI-3917999, EBI-2565740;
Q6MX51:Rv0296c (xeno); NbExp=3; IntAct=EBI-3917999, EBI-11740572;
P98066:TNFAIP6; NbExp=15; IntAct=EBI-3917999, EBI-11700693;
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: By ER stress in a DDIT3/CHOP-dependent manner.
{ECO:0000269|PubMed:20829347}.
-!- PTM: Several N-terminal processed forms are produced by
proteolytic cleavage after secretion from at least peripheral
blood monocytes, leukcocytes and endothelial cells. In general,
IL-8(1-77) is referred to as interleukin-8. IL-8(6-77) is the most
promiment form. {ECO:0000269|PubMed:11023497,
ECO:0000269|PubMed:11978786, ECO:0000269|PubMed:2145175,
ECO:0000269|PubMed:2212672, ECO:0000269|PubMed:2523801,
ECO:0000269|PubMed:2648135}.
-!- PTM: Citrullination at Arg-27 prevents proteolysis, and dampens
tissue inflammation, it also enhances leukocytosis, possibly
through impaired chemokine clearance from the blood circulation.
{ECO:0000269|PubMed:18710930, ECO:0000269|PubMed:19608678}.
-!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK00048.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-8 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_8";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il8/";
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EMBL; M17017; AAA35611.1; -; mRNA.
EMBL; Y00787; CAA68742.1; -; mRNA.
EMBL; M28130; AAA59158.1; -; Genomic_DNA.
EMBL; M26383; AAA36323.1; -; mRNA.
EMBL; D14283; BAA03245.1; -; Genomic_DNA.
EMBL; BT007067; AAP35730.1; -; mRNA.
EMBL; AK311874; BAG34815.1; -; mRNA.
EMBL; CR542151; CAG46948.1; -; mRNA.
EMBL; AF385628; AAK60276.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471057; EAX05688.1; -; Genomic_DNA.
EMBL; BC013615; AAH13615.1; -; mRNA.
EMBL; Z11686; CAA77745.1; -; mRNA.
EMBL; AF043337; AAK00048.1; ALT_SEQ; mRNA.
CCDS; CCDS34005.1; -.
PIR; A37034; A37034.
RefSeq; NP_000575.1; NM_000584.3.
PDB; 1ICW; X-ray; 2.01 A; A/B=28-99.
PDB; 1IKL; NMR; -; A=28-99.
PDB; 1IKM; NMR; -; A=28-99.
PDB; 1IL8; NMR; -; A/B=28-99.
PDB; 1ILP; NMR; -; A/B=28-99.
PDB; 1ILQ; NMR; -; A/B=28-99.
PDB; 1QE6; X-ray; 2.35 A; A/B/C/D=28-99.
PDB; 1ROD; NMR; -; A/B=28-80.
PDB; 2IL8; NMR; -; A/B=28-99.
PDB; 3IL8; X-ray; 2.00 A; A=28-99.
PDB; 4XDX; X-ray; 0.95 A; A=30-99.
PDB; 5D14; X-ray; 1.00 A; A=30-99.
PDB; 5WDZ; NMR; -; A=28-93.
PDBsum; 1ICW; -.
PDBsum; 1IKL; -.
PDBsum; 1IKM; -.
PDBsum; 1IL8; -.
PDBsum; 1ILP; -.
PDBsum; 1ILQ; -.
PDBsum; 1QE6; -.
PDBsum; 1ROD; -.
PDBsum; 2IL8; -.
PDBsum; 3IL8; -.
PDBsum; 4XDX; -.
PDBsum; 5D14; -.
PDBsum; 5WDZ; -.
SMR; P10145; -.
BioGrid; 109790; 14.
DIP; DIP-3778N; -.
IntAct; P10145; 13.
STRING; 9606.ENSP00000306512; -.
BindingDB; P10145; -.
ChEMBL; CHEMBL2157; -.
DrugBank; DB05434; ABT-510.
DrugBank; DB05484; MDX-018.
DrugBank; DB05855; Rivanicline.
DrugBank; DB06083; Tapinarof.
DrugCentral; P10145; -.
BioMuta; CXCL8; -.
DMDM; 124359; -.
EPD; P10145; -.
MassIVE; P10145; -.
PaxDb; P10145; -.
PeptideAtlas; P10145; -.
PRIDE; P10145; -.
ABCD; P10145; -.
DNASU; 3576; -.
Ensembl; ENST00000307407; ENSP00000306512; ENSG00000169429.
GeneID; 3576; -.
KEGG; hsa:3576; -.
UCSC; uc003hhe.3; human.
CTD; 3576; -.
DisGeNET; 3576; -.
GeneCards; CXCL8; -.
HGNC; HGNC:6025; CXCL8.
HPA; HPA057179; -.
MIM; 146930; gene.
neXtProt; NX_P10145; -.
OpenTargets; ENSG00000169429; -.
PharmGKB; PA29841; -.
eggNOG; ENOG410J24U; Eukaryota.
eggNOG; ENOG410Z1BP; LUCA.
GeneTree; ENSGT00940000160757; -.
InParanoid; P10145; -.
KO; K10030; -.
OMA; CANSEII; -.
OrthoDB; 1471901at2759; -.
PhylomeDB; P10145; -.
TreeFam; TF333433; -.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
SIGNOR; P10145; -.
ChiTaRS; CXCL8; human.
EvolutionaryTrace; P10145; -.
GeneWiki; Interleukin_8; -.
GenomeRNAi; 3576; -.
Pharos; P10145; -.
PMAP-CutDB; P10145; -.
PRO; PR:P10145; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000169429; Expressed in 176 organ(s), highest expression level in periodontal ligament.
ExpressionAtlas; P10145; baseline and differential.
Genevisible; P10145; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
GO; GO:0005153; F:interleukin-8 receptor binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; TAS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; TAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0006935; P:chemotaxis; TAS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0048566; P:embryonic digestive tract development; IEP:DFLAT.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0050930; P:induction of positive chemotaxis; IGI:UniProtKB.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0030595; P:leukocyte chemotaxis; IBA:GO_Central.
GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
GO; GO:0036499; P:PERK-mediated unfolded protein response; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:CACAO.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; TAS:BHF-UCL.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
GO; GO:2000535; P:regulation of entry of bacterium into host cell; IMP:AgBase.
GO; GO:0045091; P:regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0002237; P:response to molecule of bacterial origin; IDA:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00273; Chemokine_CXC; 1.
InterPro; IPR001089; Chemokine_CXC.
InterPro; IPR018048; Chemokine_CXC_CS.
InterPro; IPR001811; Chemokine_IL8-like_dom.
InterPro; IPR033899; CXC_Chemokine_domain.
InterPro; IPR028469; Interleukin-8.
InterPro; IPR036048; Interleukin_8-like_sf.
PANTHER; PTHR10179; PTHR10179; 1.
PANTHER; PTHR10179:SF42; PTHR10179:SF42; 1.
Pfam; PF00048; IL8; 1.
PRINTS; PR00437; SMALLCYTKCXC.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
1: Evidence at protein level;
3D-structure; Chemotaxis; Citrullination; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Inflammatory response;
Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:2145175,
ECO:0000269|PubMed:2523801,
ECO:0000269|PubMed:2648135}.
CHAIN 21 99 MDNCF-a.
/FTId=PRO_0000005126.
CHAIN 23 99 Interleukin-8.
/FTId=PRO_0000005127.
CHAIN 27 99 IL-8(5-77).
/FTId=PRO_0000041948.
CHAIN 28 99 IL-8(6-77).
/FTId=PRO_0000005128.
CHAIN 29 99 IL-8(7-77).
/FTId=PRO_0000005129.
CHAIN 30 99 IL-8(8-77).
/FTId=PRO_0000005130.
CHAIN 31 99 IL-8(9-77).
/FTId=PRO_0000005131.
SITE 27 28 Cleavage; by thrombin. {ECO:0000305}.
SITE 28 29 Cleavage; by MMP9.
MOD_RES 27 27 Citrulline. {ECO:0000269|PubMed:18710930,
ECO:0000269|PubMed:19608678}.
DISULFID 34 61
DISULFID 36 77
CONFLICT 53 53 R -> L (in Ref. 17; AA sequence).
{ECO:0000305}.
STRAND 37 42 {ECO:0000244|PDB:1ROD}.
HELIX 46 48 {ECO:0000244|PDB:4XDX}.
STRAND 49 55 {ECO:0000244|PDB:4XDX}.
STRAND 58 60 {ECO:0000244|PDB:1ICW}.
STRAND 61 63 {ECO:0000244|PDB:4XDX}.
STRAND 65 70 {ECO:0000244|PDB:4XDX}.
TURN 71 73 {ECO:0000244|PDB:1IKL}.
STRAND 75 78 {ECO:0000244|PDB:4XDX}.
HELIX 83 97 {ECO:0000244|PDB:4XDX}.
SEQUENCE 99 AA; 11098 MW; 15C649996E89319F CRC64;
MTSKLAVALL AAFLISAALC EGAVLPRSAK ELRCQCIKTY SKPFHPKFIK ELRVIESGPH
CANTEIIVKL SDGRELCLDP KENWVQRVVE KFLKRAENS


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