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Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (CD antigen CD11a)

 ITAL_HUMAN              Reviewed;        1170 AA.
P20701; O43746; Q45H73; Q96HB1; Q9UBC8;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
07-FEB-2006, sequence version 3.
17-JUN-2020, entry version 216.
RecName: Full=Integrin alpha-L;
AltName: Full=CD11 antigen-like family member A;
AltName: Full=Leukocyte adhesion glycoprotein LFA-1 alpha chain;
Short=LFA-1A;
AltName: Full=Leukocyte function-associated molecule 1 alpha chain;
AltName: CD_antigen=CD11a;
Flags: Precursor;
Name=ITGAL; Synonyms=CD11A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 120-132;
226-237; 282-288; 433-441; 522-531; 569-582; 591-604; 831-844 AND 957-974,
DOMAIN, AND VARIANT TRP-214.
PubMed=2537322; DOI=10.1083/jcb.108.2.703;
Larson R.S., Corbi A.L., Berman L., Springer T.;
"Primary structure of the leukocyte function-associated molecule-1 alpha
subunit: an integrin with an embedded domain defining a protein
superfamily.";
J. Cell Biol. 108:703-712(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-144; TRP-214; LYS-746
AND THR-791.
NIEHS SNPs program;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2), AND VARIANT
TRP-214.
PubMed=10493829; DOI=10.1006/geno.1999.5927;
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from human
chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
Myers R.M., Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lymph;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
PubMed=8099450; DOI=10.1073/pnas.90.11.5364;
Shelley C.S., Farokhzad O.C., Arnaout M.A.;
"Identification of cell-specific and developmentally regulated nuclear
factors that direct myeloid and lymphoid expression of the CD11a gene.";
Proc. Natl. Acad. Sci. U.S.A. 90:5364-5368(1993).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
PubMed=8103515;
Nueda A., Lopez-Cabrera M., Vara A., Corbi A.L.;
"Characterization of the CD11a (alpha L, LFA-1 alpha) integrin gene
promoter.";
J. Biol. Chem. 268:19305-19311(1993).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
PubMed=8097887; DOI=10.1073/pnas.90.9.4221;
Cornwell R.D., Gollahon K.A., Hickstein D.D.;
"Description of the leukocyte function-associated antigen 1 (LFA-1 or
CD11a) promoter.";
Proc. Natl. Acad. Sci. U.S.A. 90:4221-4225(1993).
[10]
FUNCTION.
PubMed=11812992; DOI=10.1038/ni755;
Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.;
"JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in
transendothelial migration of leukocytes.";
Nat. Immunol. 3:151-158(2002).
[11]
FUNCTION.
PubMed=15356110; DOI=10.4049/jimmunol.173.6.3653;
Barber D.F., Faure M., Long E.O.;
"LFA-1 contributes an early signal for NK cell cytotoxicity.";
J. Immunol. 173:3653-3659(2004).
[12]
DOMAIN, AND FUNCTION.
PubMed=15528364; DOI=10.4049/jimmunol.173.10.6259;
Fraemohs L., Koenen R.R., Ostermann G., Heinemann B., Weber C.;
"The functional interaction of the beta 2 integrin lymphocyte function-
associated antigen-1 with junctional adhesion molecule-A is mediated by the
I domain.";
J. Immunol. 173:6259-6264(2004).
[13]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1165, AND
MUTAGENESIS OF SER-1165.
PubMed=16301335; DOI=10.1083/jcb.200504016;
Fagerholm S.C., Hilden T.J., Nurmi S.M., Gahmberg C.G.;
"Specific integrin alpha and beta chain phosphorylations regulate LFA-1
activation through affinity-dependent and -independent mechanisms.";
J. Cell Biol. 171:705-715(2005).
[14]
INTERACTION WITH SARS VIRUS PROTEIN 7A (MICROBIAL INFECTION).
PubMed=18020948; DOI=10.1515/bc.2007.157;
Haenel K., Willbold D.;
"SARS-CoV accessory protein 7a directly interacts with human LFA-1.";
Biol. Chem. 388:1325-1332(2007).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-linked
cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[16]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23775590; DOI=10.1007/s10495-013-0873-z;
Kristof E., Zahuczky G., Katona K., Doro Z., Nagy E., Fesues L.;
"Novel role of ICAM3 and LFA-1 in the clearance of apoptotic neutrophils by
human macrophages.";
Apoptosis 18:1235-1251(2013).
[17]
INTERACTION WITH THBD.
PubMed=27055590; DOI=10.1016/j.bbrc.2016.04.007;
Kawamoto E., Okamoto T., Takagi Y., Honda G., Suzuki K., Imai H.,
Shimaoka M.;
"LFA-1 and Mac-1 integrins bind to the serine/threonine-rich domain of
thrombomodulin.";
Biochem. Biophys. Res. Commun. 473:1005-1012(2016).
[18]
FUNCTION.
PubMed=29100055; DOI=10.1016/j.molcel.2017.10.003;
Swaim C.D., Scott A.F., Canadeo L.A., Huibregtse J.M.;
"Extracellular ISG15 signals cytokine secretion through the LFA-1 integrin
receptor.";
Mol. Cell 68:581-590(2017).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, AND SEQUENCE REVISION TO
214.
PubMed=7479767; DOI=10.1073/pnas.92.22.10277;
Qu A., Leahy D.J.;
"Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta
2) integrin.";
Proc. Natl. Acad. Sci. U.S.A. 92:10277-10281(1995).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-335.
PubMed=8805579; DOI=10.1016/s0969-2126(96)00100-1;
Qu A., Leahy D.J.;
"The role of the divalent cation in the structure of the I domain from the
CD11a/CD18 integrin.";
Structure 4:931-942(1996).
[21]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 153-334.
PubMed=10493852; DOI=10.1006/jmbi.1999.3047;
Kallen J., Welzenbach K., Ramage P., Geyl D., Kriwacki R., Legge G.,
Cottens S., Weitz-Schmidt G., Hommel U.;
"Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a
I-domain.";
J. Mol. Biol. 292:1-9(1999).
[22]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH ICAM1.
PubMed=12526797; DOI=10.1016/s0092-8674(02)01257-6;
Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A.,
Zhang R., Joachimiak A., Takagi J., Wang J.H., Springer T.A.;
"Structures of the alpha L I domain and its complex with ICAM-1 reveal a
shape-shifting pathway for integrin regulation.";
Cell 112:99-111(2003).
-!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3
and ICAM4. Integrin ITGAL/ITGB2 is a receptor for F11R
(PubMed:11812992, PubMed:15528364). Integin ITGAL/ITGB2 is a receptor
for the secreted form of ubiquitin-like protein ISG15; the interaction
is mediated by ITGAL (PubMed:29100055). Involved in a variety of immune
phenomena including leukocyte-endothelial cell interaction, cytotoxic
T-cell mediated killing, and antibody dependent killing by granulocytes
and monocytes. Contributes to natural killer cell cytotoxicity
(PubMed:15356110). Involved in leukocyte adhesion and transmigration of
leukocytes including T-cells and neutrophils (PubMed:11812992).
Required for generation of common lymphoid progenitor cells in bone
marrow, indicating a role in lymphopoiesis (By similarity). Integrin
ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic
neutrophil phagocytosis by macrophages (PubMed:23775590).
{ECO:0000250|UniProtKB:P24063, ECO:0000269|PubMed:11812992,
ECO:0000269|PubMed:15356110, ECO:0000269|PubMed:15528364,
ECO:0000269|PubMed:23775590, ECO:0000269|PubMed:29100055}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:12526797).
The ITGAL alpha subunit associates with the ITGB2 beta subunit
(PubMed:12526797). Interacts with THBD (PubMed:27055590).
{ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:27055590}.
-!- SUBUNIT: (Microbial infection) Interacts with SARS virus protein 7a.
{ECO:0000269|PubMed:18020948}.
-!- INTERACTION:
P20701; P05362: ICAM1; NbExp=2; IntAct=EBI-961214, EBI-1035358;
P20701; P08575: PTPRC; NbExp=2; IntAct=EBI-961214, EBI-1341;
P20701; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-961214, EBI-6863748;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16301335};
Single-pass type I membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P20701-1; Sequence=Displayed;
Name=2;
IsoId=P20701-2; Sequence=VSP_002738;
Name=3;
IsoId=P20701-3; Sequence=VSP_042842, VSP_042843;
-!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000269|PubMed:16301335,
ECO:0000269|PubMed:23775590}.
-!- DOMAIN: The integrin I-domain (insert) is a VWFA domain
(PubMed:2537322). Integrins with I-domains do not undergo protease
cleavage. The I-domain is necessary and sufficient for interaction with
ICAM1 and F11R (PubMed:15528364). {ECO:0000269|PubMed:15528364,
ECO:0000269|PubMed:2537322}.
-!- PTM: In resting T-cells, up to 40% of surface ITGAL is constitutively
phosphorylated. Phosphorylation causes conformational changes needed
for ligand binding and is necessary for activation by some
physiological agents. {ECO:0000269|PubMed:16301335}.
-!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/itgal/";
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EMBL; Y00796; CAA68747.1; -; mRNA.
EMBL; DQ131904; AAZ38713.1; -; Genomic_DNA.
EMBL; AC002310; AAC31672.1; -; Genomic_DNA.
EMBL; AC116348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471192; EAW52243.1; -; Genomic_DNA.
EMBL; BC008777; AAH08777.1; -; mRNA.
EMBL; M95609; AAA16474.2; -; Genomic_DNA.
EMBL; Z22804; CAA80461.1; -; Genomic_DNA.
EMBL; M87662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS32433.1; -. [P20701-1]
CCDS; CCDS45461.1; -. [P20701-3]
PIR; S03308; S03308.
RefSeq; NP_001107852.1; NM_001114380.1. [P20701-3]
RefSeq; NP_002200.2; NM_002209.2. [P20701-1]
PDB; 1CQP; X-ray; 2.60 A; A/B=153-334.
PDB; 1DGQ; NMR; -; A=152-336.
PDB; 1IJ4; Model; -; L=153-333.
PDB; 1LFA; X-ray; 1.80 A; A/B=150-336.
PDB; 1MJN; X-ray; 1.30 A; A=153-331.
PDB; 1MQ8; X-ray; 3.30 A; B/D=155-331.
PDB; 1MQ9; X-ray; 2.00 A; A=153-331.
PDB; 1MQA; X-ray; 2.50 A; A=153-331.
PDB; 1RD4; X-ray; 2.40 A; A/B/C/D=150-336.
PDB; 1T0P; X-ray; 1.66 A; A=153-326.
PDB; 1XDD; X-ray; 2.20 A; A/B=152-336.
PDB; 1XDG; X-ray; 2.10 A; A/B=152-336.
PDB; 1XUO; X-ray; 1.80 A; A/B=152-336.
PDB; 1ZON; X-ray; 2.00 A; A=150-336.
PDB; 1ZOO; X-ray; 3.00 A; A/B=150-336.
PDB; 1ZOP; X-ray; 2.00 A; A/B=150-336.
PDB; 2ICA; X-ray; 1.56 A; A=154-332.
PDB; 2K8O; NMR; -; A=1113-1170.
PDB; 2M3E; NMR; -; A=1082-1128.
PDB; 2O7N; X-ray; 1.75 A; A=154-332.
PDB; 3BN3; X-ray; 2.10 A; A=154-332.
PDB; 3BQM; X-ray; 1.95 A; B/C=153-334.
PDB; 3BQN; X-ray; 1.80 A; B/C=153-334.
PDB; 3E2M; X-ray; 2.00 A; A/B=152-334.
PDB; 3EOA; X-ray; 2.80 A; I/J=153-333.
PDB; 3EOB; X-ray; 3.60 A; I/J=153-333.
PDB; 3F74; X-ray; 1.70 A; A/B/C=153-332.
PDB; 3F78; X-ray; 1.60 A; A/B/C=153-332.
PDB; 3HI6; X-ray; 2.30 A; A/B=153-332.
PDB; 3M6F; X-ray; 1.85 A; A=154-332.
PDB; 3TCX; X-ray; 3.60 A; B/D/F/H/J/L/N/P/R/T/V/X/Z/b=154-332.
PDB; 4IXD; X-ray; 1.80 A; A=152-336.
PDB; 5E6R; X-ray; 2.90 A; A=26-770.
PDB; 5E6S; X-ray; 2.15 A; A/C/E=26-770.
PDB; 5E6U; X-ray; 2.50 A; A=26-770.
PDB; 6BXB; X-ray; 2.39 A; A/B=153-331.
PDB; 6BXF; X-ray; 3.20 A; A/B=153-331.
PDB; 6BXJ; X-ray; 2.09 A; A=153-331.
PDB; 6CKB; X-ray; 2.80 A; A/B=153-331.
PDBsum; 1CQP; -.
PDBsum; 1DGQ; -.
PDBsum; 1IJ4; -.
PDBsum; 1LFA; -.
PDBsum; 1MJN; -.
PDBsum; 1MQ8; -.
PDBsum; 1MQ9; -.
PDBsum; 1MQA; -.
PDBsum; 1RD4; -.
PDBsum; 1T0P; -.
PDBsum; 1XDD; -.
PDBsum; 1XDG; -.
PDBsum; 1XUO; -.
PDBsum; 1ZON; -.
PDBsum; 1ZOO; -.
PDBsum; 1ZOP; -.
PDBsum; 2ICA; -.
PDBsum; 2K8O; -.
PDBsum; 2M3E; -.
PDBsum; 2O7N; -.
PDBsum; 3BN3; -.
PDBsum; 3BQM; -.
PDBsum; 3BQN; -.
PDBsum; 3E2M; -.
PDBsum; 3EOA; -.
PDBsum; 3EOB; -.
PDBsum; 3F74; -.
PDBsum; 3F78; -.
PDBsum; 3HI6; -.
PDBsum; 3M6F; -.
PDBsum; 3TCX; -.
PDBsum; 4IXD; -.
PDBsum; 5E6R; -.
PDBsum; 5E6S; -.
PDBsum; 5E6U; -.
PDBsum; 6BXB; -.
PDBsum; 6BXF; -.
PDBsum; 6BXJ; -.
PDBsum; 6CKB; -.
SMR; P20701; -.
BioGRID; 109889; 7.
ComplexPortal; CPX-1825; Integrin alphaL-beta2 complex.
DIP; DIP-623N; -.
IntAct; P20701; 9.
MINT; P20701; -.
STRING; 9606.ENSP00000349252; -.
BindingDB; P20701; -.
ChEMBL; CHEMBL1803; -.
DrugBank; DB04724; (S)-2-((S)-3-isobutyl-2,5-dioxo-4-quinolin-3-ylmethyl-[1,4]diazepan-1yl)-N-methyl-3-naphtalen-2-yl-propionamide.
DrugBank; DB02177; 1-Acetyl-4-(4-{4-[(2-Ethoxyphenyl)Thio]-3-Nitrophenyl}Pyridin-2-Yl)Piperazine.
DrugBank; DB07486; 3-({4-[(1E)-3-morpholin-4-yl-3-oxoprop-1-en-1-yl]-2,3-bis(trifluoromethyl)phenyl}sulfanyl)aniline.
DrugBank; DB06972; 7A-[(4-cyanophenyl)methyl]-6-(3,5-dichlorophenyl)-5-oxo-2,3,5,7A-tetrahydro-1H-pyrrolo[1,2-A]pyrrole-7-carbonitrile.
DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DrugBank; DB00095; Efalizumab.
DrugBank; DB03932; LFA703.
DrugBank; DB11611; Lifitegrast.
DrugBank; DB00227; Lovastatin.
DrugBank; DB08860; Pitavastatin.
DrugBank; DB01098; Rosuvastatin.
DrugBank; DB00641; Simvastatin.
DrugCentral; P20701; -.
GuidetoPHARMACOLOGY; 2451; -.
GlyConnect; 1410; -.
iPTMnet; P20701; -.
PhosphoSitePlus; P20701; -.
BioMuta; ITGAL; -.
DMDM; 88911345; -.
jPOST; P20701; -.
MassIVE; P20701; -.
MaxQB; P20701; -.
PaxDb; P20701; -.
PeptideAtlas; P20701; -.
PRIDE; P20701; -.
ProteomicsDB; 53774; -. [P20701-1]
ProteomicsDB; 53775; -. [P20701-2]
ProteomicsDB; 53776; -. [P20701-3]
ABCD; P20701; 31 sequenced antibodies.
Antibodypedia; 13698; 2034 antibodies.
DNASU; 3683; -.
Ensembl; ENST00000356798; ENSP00000349252; ENSG00000005844. [P20701-1]
Ensembl; ENST00000358164; ENSP00000350886; ENSG00000005844. [P20701-3]
GeneID; 3683; -.
KEGG; hsa:3683; -.
UCSC; uc002dyi.5; human. [P20701-1]
CTD; 3683; -.
DisGeNET; 3683; -.
EuPathDB; HostDB:ENSG00000005844.17; -.
GeneCards; ITGAL; -.
HGNC; HGNC:6148; ITGAL.
HPA; ENSG00000005844; Tissue enhanced (blood, lymphoid tissue).
MIM; 153370; gene.
neXtProt; NX_P20701; -.
OpenTargets; ENSG00000005844; -.
PharmGKB; PA29948; -.
eggNOG; KOG3637; Eukaryota.
eggNOG; ENOG410XPVZ; LUCA.
GeneTree; ENSGT00940000161495; -.
HOGENOM; CLU_004111_3_0_1; -.
InParanoid; P20701; -.
KO; K05718; -.
OMA; TVCFQLK; -.
PhylomeDB; P20701; -.
TreeFam; TF105391; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
SignaLink; P20701; -.
SIGNOR; P20701; -.
BioGRID-ORCS; 3683; 2 hits in 786 CRISPR screens.
ChiTaRS; ITGAL; human.
EvolutionaryTrace; P20701; -.
GeneWiki; CD11a; -.
GenomeRNAi; 3683; -.
Pharos; P20701; Tclin.
PRO; PR:P20701; -.
Proteomes; UP000005640; Chromosome 16.
RNAct; P20701; protein.
Bgee; ENSG00000005844; Expressed in leukocyte and 209 other tissues.
ExpressionAtlas; P20701; baseline and differential.
Genevisible; P20701; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0034687; C:integrin alphaL-beta2 complex; IDA:UniProtKB.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0050839; F:cell adhesion molecule binding; IMP:UniProtKB.
GO; GO:0030369; F:ICAM-3 receptor activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; ISS:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:BHF-UCL.
GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:ARUK-UCL.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0035683; P:memory T cell extravasation; IDA:ARUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:BHF-UCL.
Gene3D; 2.130.10.130; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR028994; Integrin_alpha_N.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF01839; FG-GAP; 1.
Pfam; PF00357; Integrin_alpha; 1.
Pfam; PF08441; Integrin_alpha2; 1.
Pfam; PF00092; VWA; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 2.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding;
Phagocytosis; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1..25
/evidence="ECO:0000255"
CHAIN 26..1170
/note="Integrin alpha-L"
/id="PRO_0000016292"
TOPO_DOM 26..1090
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1091..1111
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1112..1170
/note="Cytoplasmic"
/evidence="ECO:0000255"
REPEAT 31..82
/note="FG-GAP 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
REPEAT 83..141
/note="FG-GAP 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
DOMAIN 156..327
/note="VWFA"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
REPEAT 338..389
/note="FG-GAP 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
REPEAT 390..445
/note="FG-GAP 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
REPEAT 446..506
/note="FG-GAP 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
REPEAT 507..563
/note="FG-GAP 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
REPEAT 567..627
/note="FG-GAP 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
CA_BIND 468..476
/evidence="ECO:0000255"
CA_BIND 530..538
/evidence="ECO:0000255"
CA_BIND 590..598
/evidence="ECO:0000255"
MOTIF 1115..1119
/note="GFFKR motif"
MOD_RES 1165
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:16301335"
CARBOHYD 65
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 89
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 188
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973"
CARBOHYD 649
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 670
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 726
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 730
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 862
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 885
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 897
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1060
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1071
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 73..80
/evidence="ECO:0000250"
DISULFID 111..129
/evidence="ECO:0000250"
DISULFID 653..707
/evidence="ECO:0000250"
DISULFID 771..777
/evidence="ECO:0000250"
DISULFID 845..861
/evidence="ECO:0000250"
DISULFID 998..1013
/evidence="ECO:0000250"
DISULFID 1021..1052
/evidence="ECO:0000250"
VAR_SEQ 110..192
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_042842"
VAR_SEQ 746
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_042843"
VAR_SEQ 954
/note="Q -> QGVHGLVEMQTSKQILCRPAGDAEHTVGAQEGELPCPWGVSEAFRDN
IRAGPCR (in isoform 2)"
/evidence="ECO:0000305"
/id="VSP_002738"
VARIANT 144
/note="R -> H (in dbSNP:rs34166708)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_025235"
VARIANT 214
/note="R -> W (in dbSNP:rs1064524)"
/evidence="ECO:0000269|PubMed:10493829,
ECO:0000269|PubMed:2537322, ECO:0000269|Ref.2"
/id="VAR_025236"
VARIANT 746
/note="Q -> K (in dbSNP:rs34838942)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_025237"
VARIANT 791
/note="R -> T (in dbSNP:rs2230433)"
/evidence="ECO:0000269|Ref.2"
/id="VAR_025238"
MUTAGEN 1165
/note="S->A: Abolishes phosphorylation and MEM-83-activated
T-cell adhesion to ICAM1. Abolishes integrin alpha-L/beta-2
activation by CXCL12 and TERF2IP/RAP1. Does not affect
heterodimerization of cell surface expression. Does not
affect TCR- or phorbol ester-activated T-cell adhesion to
ICAM1."
/evidence="ECO:0000269|PubMed:16301335"
CONFLICT 660
/note="I -> Y (in Ref. 1; CAA68747)"
/evidence="ECO:0000305"
HELIX 30..32
/evidence="ECO:0000244|PDB:5E6U"
STRAND 34..36
/evidence="ECO:0000244|PDB:5E6S"
TURN 43..46
/evidence="ECO:0000244|PDB:5E6S"
STRAND 47..52
/evidence="ECO:0000244|PDB:5E6S"
STRAND 55..60
/evidence="ECO:0000244|PDB:5E6S"
STRAND 69..73
/evidence="ECO:0000244|PDB:5E6S"
TURN 75..77
/evidence="ECO:0000244|PDB:5E6S"
STRAND 80..82
/evidence="ECO:0000244|PDB:5E6S"
TURN 93..96
/evidence="ECO:0000244|PDB:5E6S"
STRAND 97..101
/evidence="ECO:0000244|PDB:5E6S"
TURN 103..105
/evidence="ECO:0000244|PDB:5E6S"
STRAND 108..119
/evidence="ECO:0000244|PDB:5E6S"
STRAND 122..134
/evidence="ECO:0000244|PDB:5E6S"
STRAND 140..143
/evidence="ECO:0000244|PDB:5E6S"
STRAND 155..162
/evidence="ECO:0000244|PDB:1MJN"
HELIX 169..185
/evidence="ECO:0000244|PDB:1MJN"
TURN 186..188
/evidence="ECO:0000244|PDB:1MJN"
STRAND 189..206
/evidence="ECO:0000244|PDB:1MJN"
HELIX 208..214
/evidence="ECO:0000244|PDB:1MJN"
HELIX 217..221
/evidence="ECO:0000244|PDB:1MJN"
HELIX 233..243
/evidence="ECO:0000244|PDB:1MJN"
HELIX 247..249
/evidence="ECO:0000244|PDB:1MJN"
STRAND 255..265
/evidence="ECO:0000244|PDB:1MJN"
HELIX 274..276
/evidence="ECO:0000244|PDB:1MJN"
STRAND 279..287
/evidence="ECO:0000244|PDB:1MJN"
HELIX 288..290
/evidence="ECO:0000244|PDB:1MJN"
HELIX 293..297
/evidence="ECO:0000244|PDB:1MJN"
HELIX 298..302
/evidence="ECO:0000244|PDB:1MJN"
HELIX 307..310
/evidence="ECO:0000244|PDB:1MJN"
STRAND 311..316
/evidence="ECO:0000244|PDB:1MJN"
HELIX 317..319
/evidence="ECO:0000244|PDB:1MJN"
HELIX 323..330
/evidence="ECO:0000244|PDB:1MJN"
STRAND 331..333
/evidence="ECO:0000244|PDB:3BQN"
STRAND 352..359
/evidence="ECO:0000244|PDB:5E6S"
STRAND 362..367
/evidence="ECO:0000244|PDB:5E6S"
HELIX 370..373
/evidence="ECO:0000244|PDB:5E6S"
STRAND 375..380
/evidence="ECO:0000244|PDB:5E6S"
STRAND 387..391
/evidence="ECO:0000244|PDB:5E6S"
TURN 398..401
/evidence="ECO:0000244|PDB:5E6S"
STRAND 406..411
/evidence="ECO:0000244|PDB:5E6S"
STRAND 413..416
/evidence="ECO:0000244|PDB:5E6S"
STRAND 419..424
/evidence="ECO:0000244|PDB:5E6S"
HELIX 427..429
/evidence="ECO:0000244|PDB:5E6S"
STRAND 432..437
/evidence="ECO:0000244|PDB:5E6S"
STRAND 446..452
/evidence="ECO:0000244|PDB:5E6S"
STRAND 462..467
/evidence="ECO:0000244|PDB:5E6S"
STRAND 472..474
/evidence="ECO:0000244|PDB:5E6S"
STRAND 477..482
/evidence="ECO:0000244|PDB:5E6S"
STRAND 493..499
/evidence="ECO:0000244|PDB:5E6S"
STRAND 501..510
/evidence="ECO:0000244|PDB:5E6S"
STRAND 514..516
/evidence="ECO:0000244|PDB:5E6S"
STRAND 523..527
/evidence="ECO:0000244|PDB:5E6S"
STRAND 531..535
/evidence="ECO:0000244|PDB:5E6S"
STRAND 539..543
/evidence="ECO:0000244|PDB:5E6S"
STRAND 549..554
/evidence="ECO:0000244|PDB:5E6S"
STRAND 558..561
/evidence="ECO:0000244|PDB:5E6R"
STRAND 566..570
/evidence="ECO:0000244|PDB:5E6S"
HELIX 571..574
/evidence="ECO:0000244|PDB:5E6S"
STRAND 583..589
/evidence="ECO:0000244|PDB:5E6S"
STRAND 593..595
/evidence="ECO:0000244|PDB:5E6S"
STRAND 598..603
/evidence="ECO:0000244|PDB:5E6S"
STRAND 606..612
/evidence="ECO:0000244|PDB:5E6S"
TURN 1082..1086
/evidence="ECO:0000244|PDB:2M3E"
HELIX 1090..1114
/evidence="ECO:0000244|PDB:2M3E"
HELIX 1118..1123
/evidence="ECO:0000244|PDB:2K8O"
TURN 1124..1127
/evidence="ECO:0000244|PDB:2K8O"
HELIX 1137..1147
/evidence="ECO:0000244|PDB:2K8O"
HELIX 1153..1155
/evidence="ECO:0000244|PDB:2K8O"
HELIX 1156..1165
/evidence="ECO:0000244|PDB:2K8O"
HELIX 1167..1170
/evidence="ECO:0000244|PDB:2K8O"
SEQUENCE 1170 AA; 128770 MW; 22A7AF92EF286876 CRC64;
MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL QVGNGVIVGA
PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA TDPTDGSILA CDPGLSRTCD
QNTYLSGLCY LFRQNLQGPM LQGRPGFQEC IKGNVDLVFL FDGSMSLQPD EFQKILDFMK
DVMKKLSNTS YQFAAVQFST SYKTEFDFSD YVKRKDPDAL LKHVKHMLLL TNTFGAINYV
ATEVFREELG ARPDATKVLI IITDGEATDS GNIDAAKDII RYIIGIGKHF QTKESQETLH
KFASKPASEF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFNMELS SSGISADLSR
GHAVVGAVGA KDWAGGFLDL KADLQDDTFI GNEPLTPEVR AGYLGYTVTW LPSRQKTSLL
ASGAPRYQHM GRVLLFQEPQ GGGHWSQVQT IHGTQIGSYF GGELCGVDVD QDGETELLLI
GAPLFYGEQR GGRVFIYQRR QLGFEEVSEL QGDPGYPLGR FGEAITALTD INGDGLVDVA
VGAPLEEQGA VYIFNGRHGG LSPQPSQRIE GTQVLSGIQW FGRSIHGVKD LEGDGLADVA
VGAESQMIVL SSRPVVDMVT LMSFSPAEIP VHEVECSYST SNKMKEGVNI TICFQIKSLI
PQFQGRLVAN LTYTLQLDGH RTRRRGLFPG GRHELRRNIA VTTSMSCTDF SFHFPVCVQD
LISPINVSLN FSLWEEEGTP RDQRAQGKDI PPILRPSLHS ETWEIPFEKN CGEDKKCEAN
LRVSFSPARS RALRLTAFAS LSVELSLSNL EEDAYWVQLD LHFPPGLSFR KVEMLKPHSQ
IPVSCEELPE ESRLLSRALS CNVSSPIFKA GHSVALQMMF NTLVNSSWGD SVELHANVTC
NNEDSDLLED NSATTIIPIL YPINILIQDQ EDSTLYVSFT PKGPKIHQVK HMYQVRIQPS
IHDHNIPTLE AVVGVPQPPS EGPITHQWSV QMEPPVPCHY EDLERLPDAA EPCLPGALFR
CPVVFRQEIL VQVIGTLELV GEIEASSMFS LCSSLSISFN SSKHFHLYGS NASLAQVVMK
VDVVYEKQML YLYVLSGIGG LLLLLLIFIV LYKVGFFKRN LKEKMEAGRG VPNGIPAEDS
EQLASGQEAG DPGCLKPLHE KDSESGGGKD


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