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B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a)

 CD79A_MOUSE             Reviewed;         220 AA.
P11911; Q6GTY0;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 2.
30-AUG-2017, entry version 168.
RecName: Full=B-cell antigen receptor complex-associated protein alpha chain;
AltName: Full=Ig-alpha;
AltName: Full=MB-1 membrane glycoprotein;
AltName: Full=Membrane-bound immunoglobulin-associated protein;
AltName: Full=Surface IgM-associated protein;
AltName: CD_antigen=CD79a;
Flags: Precursor;
Name=Cd79a; Synonyms=Iga, Mb-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X DBA/2J;
PubMed=2463161;
Sakaguchi N., Kashiwamura S., Kimoto M., Thalmann P., Melchers F.;
"B lymphocyte lineage-restricted expression of mb-1, a gene with CD3-
like structural properties.";
EMBO J. 7:3457-3464(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=2358676;
Kashiwamura S., Koyama T., Matsuo T., Steinmetz M., Kimoto M.,
Sakaguchi N.;
"Structure of the murine mb-1 gene encoding a putative sIgM-associated
molecule.";
J. Immunol. 145:337-343(1990).
[3]
NUCLEOTIDE SEQUENCE.
PubMed=1639443; DOI=10.1007/BF00215058;
Flaswinkel H., Reth M.;
"Molecular cloning of the Ig-alpha subunit of the human B-cell antigen
receptor complex.";
Immunogenetics 36:266-269(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
PubMed=1922076; DOI=10.1128/MCB.11.11.5756;
Travis A., Hagman J., Grosschedl R.;
"Heterogeneously initiated transcription from the pre-B- and B-cell-
specific mb-1 promoter: analysis of the requirement for upstream
factor-binding sites and initiation site sequences.";
Mol. Cell. Biol. 11:5756-5766(1991).
[6]
PROTEIN SEQUENCE OF 29-38.
PubMed=2269334; DOI=10.1002/eji.1830201239;
Hombach J., Lottspeich F., Reth M.;
"Identification of the genes encoding the IgM-alpha and Ig-beta
components of the IgM antigen receptor complex by amino-terminal
sequencing.";
Eur. J. Immunol. 20:2795-2799(1990).
[7]
PROTEIN SEQUENCE OF 29-38.
PubMed=2023945; DOI=10.1073/pnas.88.9.3982;
Campbell K.S., Hager E.J., Friedrich R.J., Cambier J.C.;
"IgM antigen receptor complex contains phosphoprotein products of B29
and mb-1 genes.";
Proc. Natl. Acad. Sci. U.S.A. 88:3982-3986(1991).
[8]
INTERACTION WITH BLK.
PubMed=1506682;
Lin J., Justement L.B.;
"The MB-1/B29 heterodimer couples the B cell antigen receptor to
multiple src family protein tyrosine kinases.";
J. Immunol. 149:1548-1555(1992).
[9]
INTERACTION WITH LYN, AND PHOSPHORYLATION.
PubMed=15335855; DOI=10.1016/0960-9822(93)90062-S;
Law D.A., Chan V.W., Datta S.K., DeFranco A.L.;
"B-cell antigen receptor motifs have redundant signalling capabilities
and bind the tyrosine kinases PTK72, Lyn and Fyn.";
Curr. Biol. 3:645-657(1993).
[10]
PHOSPHORYLATION AT TYR-182, AND MUTAGENESIS OF TYR-176; TYR-182 AND
TYR-193.
PubMed=8306975;
Flaswinkel H., Reth M.;
"Dual role of the tyrosine activation motif of the Ig-alpha protein
during signal transduction via the B cell antigen receptor.";
EMBO J. 13:83-89(1994).
[11]
INTERACTION WITH FYN AND LYN.
PubMed=8168489;
Clark M.R., Johnson S.A., Cambier J.C.;
"Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels
of binding specificity and tyrosine phosphorylated Ig-alpha
stimulation of Fyn activity.";
EMBO J. 13:1911-1919(1994).
[12]
FUNCTION.
PubMed=8175787;
Taddie J.A., Hurley T.R., Hardwick B.S., Sefton B.M.;
"Activation of B- and T-cells by the cytoplasmic domains of the B-cell
antigen receptor proteins Ig-alpha and Ig-beta.";
J. Biol. Chem. 269:13529-13535(1994).
[13]
INTERACTION WITH SYK.
PubMed=7538118; DOI=10.1074/jbc.270.19.11590;
Rowley R.B., Burkhardt A.L., Chao H.-G., Matsueda G.R., Bolen J.B.;
"Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated
Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and
autophosphorylation.";
J. Biol. Chem. 270:11590-11594(1995).
[14]
INTERACTION WITH BLK, AND PHOSPHORYLATION AT TYR-182 AND TYR-193.
PubMed=7592958; DOI=10.1074/jbc.270.45.27072;
Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B.,
Mahajan S.;
"Reconstitution of the B cell antigen receptor signaling components in
COS cells.";
J. Biol. Chem. 270:27072-27078(1995).
[15]
FUNCTION, AND MUTAGENESIS OF TYR-182 AND TYR-193.
PubMed=9469435;
Cassard S., Salamero J., Hanau D., Spehner D., Davoust J.,
Fridman W.H., Bonnerot C.;
"A tyrosine-based signal present in Ig alpha mediates B cell receptor
constitutive internalization.";
J. Immunol. 160:1767-1773(1998).
[16]
FUNCTION.
PubMed=10591178; DOI=10.1016/S1074-7613(00)80128-4;
Torres R.M., Hafen K.;
"A negative regulatory role for Ig-alpha during B cell development.";
Immunity 11:527-536(1999).
[17]
SUBCELLULAR LOCATION.
PubMed=10587346; DOI=10.1084/jem.190.11.1549;
Cheng P.C., Dykstra M.L., Mitchell R.N., Pierce S.K.;
"A role for lipid rafts in B cell antigen receptor signaling and
antigen targeting.";
J. Exp. Med. 190:1549-1560(1999).
[18]
FUNCTION.
PubMed=10352267;
Siemasko K., Eisfelder B.J., Stebbins C., Kabak S., Sant A.J.,
Song W., Clark M.R.;
"Ig alpha and Ig beta are required for efficient trafficking to late
endosomes and to enhance antigen presentation.";
J. Immunol. 162:6518-6525(1999).
[19]
INTERACTION WITH BLNK, PHOSPHORYLATION AT TYR-204, AND MUTAGENESIS OF
TYR-204.
PubMed=11449366;
DOI=10.1002/1521-4141(200107)31:7<2126::AID-IMMU2126>3.0.CO;2-O;
Engels N., Wollscheid B., Wienands J.;
"Association of SLP-65/BLNK with the B cell antigen receptor through a
non-ITAM tyrosine of Ig-alpha.";
Eur. J. Immunol. 31:2126-2134(2001).
[20]
FUNCTION, AND MUTAGENESIS OF TYR-182 AND TYR-193.
PubMed=11514602; DOI=10.1084/jem.194.4.455;
Kraus M., Pao L.I., Reichlin A., Hu Y., Canono B., Cambier J.C.,
Nussenzweig M.C., Rajewsky K.;
"Interference with immunoglobulin (Ig)alpha immunoreceptor tyrosine-
based activation motif (ITAM) phosphorylation modulates or blocks B
cell development, depending on the availability of an Igbeta
cytoplasmic tail.";
J. Exp. Med. 194:455-469(2001).
[21]
SUBCELLULAR LOCATION.
PubMed=11238609; DOI=10.4049/jimmunol.166.6.3693;
Cheng P.C., Brown B.K., Song W., Pierce S.K.;
"Translocation of the B cell antigen receptor into lipid rafts reveals
a novel step in signaling.";
J. Immunol. 166:3693-3701(2001).
[22]
FUNCTION.
PubMed=12356683; DOI=10.1093/intimm/14.10.1179;
Li C., Siemasko K., Clark M.R., Song W.;
"Cooperative interaction of Ig(alpha) and Ig(beta) of the BCR
regulates the kinetics and specificity of antigen targeting.";
Int. Immunol. 14:1179-1191(2002).
[23]
FUNCTION, INTERACTION WITH BLNK, AND MUTAGENESIS OF TYR-176 AND
TYR-204.
PubMed=11859098; DOI=10.4049/jimmunol.168.5.2127;
Siemasko K., Skaggs B.J., Kabak S., Williamson E., Brown B.K.,
Song W., Clark M.R.;
"Receptor-facilitated antigen presentation requires the recruitment of
B cell linker protein to Igalpha.";
J. Immunol. 168:2127-2138(2002).
[24]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12097390; DOI=10.4049/jimmunol.169.2.865;
Pelanda R., Braun U., Hobeika E., Nussenzweig M.C., Reth M.;
"B cell progenitors are arrested in maturation but have intact VDJ
recombination in the absence of Ig-alpha and Ig-beta.";
J. Immunol. 169:865-872(2002).
[25]
INTERACTION WITH BLNK, AND MUTAGENESIS OF TYR-176 AND TYR-204.
PubMed=11909947; DOI=10.1128/MCB.22.8.2524-2535.2002;
Kabak S., Skaggs B.J., Gold M.R., Affolter M., West K.L., Foster M.S.,
Siemasko K., Chan A.C., Aebersold R., Clark M.R.;
"The direct recruitment of BLNK to immunoglobulin alpha couples the B-
cell antigen receptor to distal signaling pathways.";
Mol. Cell. Biol. 22:2524-2535(2002).
[26]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15661879; DOI=10.4049/jimmunol.174.3.1245;
Fuentes-Panana E.M., Bannish G., van der Voort D., King L.B.,
Monroe J.G.;
"Ig alpha/Ig beta complexes generate signals for B cell development
independent of selective plasma membrane compartmentalization.";
J. Immunol. 174:1245-1252(2005).
[27]
FUNCTION, AND MUTAGENESIS OF TYR-176 AND TYR-204.
PubMed=16860757; DOI=10.1016/j.immuni.2006.04.014;
Patterson H.C.K., Kraus M., Kim Y.-M., Ploegh H., Rajewsky K.;
"The B cell receptor promotes B cell activation and proliferation
through a non-ITAM tyrosine in the Igalpha cytoplasmic domain.";
Immunity 25:55-65(2006).
[28]
FUNCTION, AND MUTAGENESIS OF TYR-176; TYR-182; TYR-193 AND TYR-204.
PubMed=17163454; DOI=10.1002/eji.200636667;
Storch B., Meixlsperger S., Jumaa H.;
"The Ig-alpha ITAM is required for efficient differentiation but not
proliferation of pre-B cells.";
Eur. J. Immunol. 37:252-260(2007).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[30]
METHYLATION AT ARG-198 BY PRMT1, AND MUTAGENESIS OF ARG-198.
PubMed=20231378; DOI=10.1084/jem.20091303;
Infantino S., Benz B., Waldmann T., Jung M., Schneider R., Reth M.;
"Arginine methylation of the B cell antigen receptor promotes
differentiation.";
J. Exp. Med. 207:711-719(2010).
-!- FUNCTION: Required in cooperation with CD79B for initiation of the
signal transduction cascade activated by binding of antigen to the
B-cell antigen receptor complex (BCR) which leads to
internalization of the complex, trafficking to late endosomes and
antigen presentation. Also required for BCR surface expression and
for efficient differentiation of pro- and pre-B-cells. Stimulates
SYK autophosphorylation and activation. Binds to BLNK, bringing
BLNK into proximity with SYK and allowing SYK to phosphorylate
BLNK. Also interacts with and increases activity of some Src-
family tyrosine kinases. Represses BCR signaling during
development of immature B-cells. {ECO:0000269|PubMed:10352267,
ECO:0000269|PubMed:10591178, ECO:0000269|PubMed:11514602,
ECO:0000269|PubMed:11859098, ECO:0000269|PubMed:12097390,
ECO:0000269|PubMed:12356683, ECO:0000269|PubMed:15661879,
ECO:0000269|PubMed:16860757, ECO:0000269|PubMed:17163454,
ECO:0000269|PubMed:8175787, ECO:0000269|PubMed:9469435}.
-!- SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked.
Part of the B-cell antigen receptor complex where the alpha/beta
chain heterodimer is non-covalently associated with an antigen-
specific membrane-bound surface immunoglobulin of two heavy chains
and two light chains. Interacts through its phosphorylated ITAM
domain with the SH2 domains of SYK which stimulates SYK
autophosphorylation and activation. Also interacts, when
phosphorylated on Tyr-204, with the SH2 domain of BLNK/SLP65,
bringing BLNK into proximity with SYK and allowing SYK to
phosphorylate BLNK which is necessary for trafficking of the BCR
to late endosomes. Interacts with Src-family tyrosine kinases
including FYN and LYN, increasing their activity.
{ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:11859098,
ECO:0000269|PubMed:11909947, ECO:0000269|PubMed:1506682,
ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:7538118,
ECO:0000269|PubMed:7592958, ECO:0000269|PubMed:8168489}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346,
ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-
pass type I membrane protein {ECO:0000269|PubMed:10587346,
ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}.
Note=Following antigen binding, the BCR has been shown to
translocate from detergent-soluble regions of the cell membrane to
lipid rafts although signal transduction through the complex can
also occur outside lipid rafts.
-!- TISSUE SPECIFICITY: B-cells.
-!- PTM: Phosphorylated on tyrosine, serine and threonine residues
upon B-cell activation. Phosphorylation of tyrosine residues by
Src-family kinases, including LYN, is an early and essential
feature of the BCR signaling cascade. The phosphorylated tyrosines
serve as docking sites for SH2-domain containing kinases, leading
to their activation which in turn leads to phosphorylation of
downstream targets. Phosphorylation of serine and threonine
residues may prevent subsequent tyrosine phosphorylation.
{ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:15335855,
ECO:0000269|PubMed:7592958, ECO:0000269|PubMed:8306975}.
-!- PTM: Arginine methylation in the ITAM domain may interfere with
the binding of SYK. It promotes signals leading to B-cell
differentiation. {ECO:0000269|PubMed:20231378}.
-!- DISRUPTION PHENOTYPE: Mice display impaired B-cell development
which does not progress pass the progenitor stage.
{ECO:0000269|PubMed:12097390}.
-----------------------------------------------------------------------
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EMBL; X13450; CAA31801.1; -; mRNA.
EMBL; M31773; AAA39494.1; -; Genomic_DNA.
EMBL; BC027633; AAH27633.1; -; mRNA.
EMBL; S59359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS20967.1; -.
PIR; A43540; A43540.
RefSeq; NP_031681.2; NM_007655.3.
UniGene; Mm.1355; -.
ProteinModelPortal; P11911; -.
SMR; P11911; -.
BioGrid; 198611; 3.
DIP; DIP-61170N; -.
ELM; P11911; -.
IntAct; P11911; 1.
STRING; 10090.ENSMUSP00000003469; -.
iPTMnet; P11911; -.
PhosphoSitePlus; P11911; -.
MaxQB; P11911; -.
PaxDb; P11911; -.
PRIDE; P11911; -.
Ensembl; ENSMUST00000003469; ENSMUSP00000003469; ENSMUSG00000003379.
GeneID; 12518; -.
KEGG; mmu:12518; -.
UCSC; uc009fqt.1; mouse.
CTD; 973; -.
MGI; MGI:101774; Cd79a.
eggNOG; ENOG410IV8X; Eukaryota.
eggNOG; ENOG4111VIC; LUCA.
GeneTree; ENSGT00510000049127; -.
HOGENOM; HOG000074307; -.
HOVERGEN; HBG050854; -.
InParanoid; P11911; -.
KO; K06506; -.
OMA; EGTKNRI; -.
OrthoDB; EOG091G10RQ; -.
PhylomeDB; P11911; -.
TreeFam; TF336032; -.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
PRO; PR:P11911; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000003379; -.
CleanEx; MM_CD79A; -.
Genevisible; P11911; MM.
GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005771; C:multivesicular body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0042113; P:B cell activation; IMP:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
Pfam; PF00047; ig; 1.
Pfam; PF02189; ITAM; 1.
SMART; SM00409; IG; 1.
SMART; SM00077; ITAM; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51055; ITAM_1; 1.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Methylation; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000269|PubMed:2023945,
ECO:0000269|PubMed:2269334}.
CHAIN 29 220 B-cell antigen receptor complex-
associated protein alpha chain.
/FTId=PRO_0000014559.
TOPO_DOM 29 137 Extracellular. {ECO:0000255}.
TRANSMEM 138 159 Helical. {ECO:0000255}.
TOPO_DOM 160 220 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 117 Ig-like C2-type.
DOMAIN 171 199 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
SITE 204 204 Required for binding to BLNK.
MOD_RES 182 182 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000255|PROSITE-ProRule:PRU00379,
ECO:0000269|PubMed:7592958,
ECO:0000269|PubMed:8306975}.
MOD_RES 193 193 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000255|PROSITE-ProRule:PRU00379,
ECO:0000269|PubMed:7592958}.
MOD_RES 198 198 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:20231378}.
MOD_RES 204 204 Phosphotyrosine; by Tyr-kinases.
{ECO:0000255|PROSITE-ProRule:PRU00379,
ECO:0000269|PubMed:11449366}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 101 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 113 113 Interchain (with C-135 in beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00114}.
MUTAGEN 176 176 Y->F: Increases tyrosine phosphorylation.
Inhibits phosphorylation of BLNK.
Impaired antigen presentation; when
associated with F-204.
{ECO:0000269|PubMed:11859098,
ECO:0000269|PubMed:11909947,
ECO:0000269|PubMed:16860757,
ECO:0000269|PubMed:17163454,
ECO:0000269|PubMed:8306975}.
MUTAGEN 182 182 Y->F: Strongly reduces tyrosine
phosphorylation and pre-B-cell
differentiation; when associated with F-
193. Abolishes constitutive
internalization of BCR.
{ECO:0000269|PubMed:11514602,
ECO:0000269|PubMed:17163454,
ECO:0000269|PubMed:8306975,
ECO:0000269|PubMed:9469435}.
MUTAGEN 193 193 Y->F: Strongly reduces tyrosine
phosphorylation and pre-B-cell
differentiation; when associated with F-
182. No effect on constitutive
internalization of BCR.
{ECO:0000269|PubMed:11514602,
ECO:0000269|PubMed:17163454,
ECO:0000269|PubMed:8306975,
ECO:0000269|PubMed:9469435}.
MUTAGEN 198 198 R->K: Associates more strongly with SYK.
Increases calcium response upon BCR
ligation. {ECO:0000269|PubMed:20231378}.
MUTAGEN 204 204 Y->F: Has little effect on tyrosine
phosphorylation. Reduces pre-B-cell
differentiation. Abolishes binding to
BLNK. Inhibits phosphorylation of BLNK.
No effect on cap formation or BCR
internalization. Impaired antigen
presentation; when associated with F-176.
{ECO:0000269|PubMed:11449366,
ECO:0000269|PubMed:11859098,
ECO:0000269|PubMed:11909947,
ECO:0000269|PubMed:16860757,
ECO:0000269|PubMed:17163454}.
CONFLICT 95 100 HRGLYW -> TGACTG (in Ref. 1; CAA31801 and
2; AAA39494). {ECO:0000305}.
SEQUENCE 220 AA; 24583 MW; A4C648C2BE6D3E38 CRC64;
MPGGLEALRA LPLLLFLSYA CLGPGCQALR VEGGPPSLTV NLGEEARLTC ENNGRNPNIT
WWFSLQSNIT WPPVPLGPGQ GTTGQLFFPE VNKNHRGLYW CQVIENNILK RSCGTYLRVR
NPVPRPFLDM GEGTKNRIIT AEGIILLFCA VVPGTLLLFR KRWQNEKFGV DMPDDYEDEN
LYEGLNLDDC SMYEDISRGL QGTYQDVGNL HIGDAQLEKP


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CSB-EL004957MO Mouse B-cell antigen receptor complex-associated protein alpha chain(CD79A) ELISA kit SpeciesMouse 96T
CSB-EL004957HU Human B-cell antigen receptor complex-associated protein alpha chain(CD79A) ELISA kit SpeciesHuman 96T
CD79A_BOVIN ELISA Kit FOR B-cell antigen receptor complex-associated protein alpha chain; organism: Bovine; gene name: CD79A 96T
CD79A_HUMAN ELISA Kit FOR B-cell antigen receptor complex-associated protein alpha chain; organism: Human; gene name: CD79A 96T
EIAAB06381 B-cell antigen receptor complex-associated protein alpha chain,Canis familiaris,Canis lupus familiaris,CD79A,Dog,Ig-alpha
32-134 CD8 T cell surface antigen is heterodimer of an alpha and a beta chain linked by two disulfide bonds .It belongs type I membrane protein. Selectively expressing of CD8 on a subset of T cells leads to 0.1 mg
EIAAB06400 Cd8b,Cd8b1,Ly-3,Lymphocyte antigen 3,Lyt3,Lyt-3,Mouse,Mus musculus,T-cell membrane glycoprotein Ly-3,T-cell surface glycoprotein CD8 beta chain,T-cell surface glycoprotein Lyt-3
EIAAB06386 B-cell antigen receptor complex-associated protein beta chain,B-cell-specific glycoprotein B29,Cd79b,Igb,Ig-beta,Immunoglobulin-associated B29 protein,Mouse,Mus musculus
EIAAB06385 B29,B-cell antigen receptor complex-associated protein beta chain,B-cell-specific glycoprotein B29,CD79B,Homo sapiens,Human,IGB,Ig-beta,Immunoglobulin-associated B29 protein
EIAAB06399 CD8 antigen 37 kDa chain,Cd8b,Cd8b1,OX-8 membrane antigen,Rat,Rattus norvegicus,T-cell surface glycoprotein CD8 beta chain
20-783-72298 MOUSE ANTI HUMAN CD11b - INTEGRIN ALPHA M CHAIN. MAC-1; Cell surface glycoprotein MAC-1 subunit alpha; CR-3 alpha chain; Leukocyte adhesion receptor MO1; Neutrophil adherence receptor; CD11b antigen M 0.2 mg
20-783-72303 MOUSE ANTI HUMAN CD11b - INTEGRIN ALPHA M CHAIN. MAC-1; Cell surface glycoprotein MAC-1 subunit alpha; CR-3 alpha chain; Leukocyte adhesion receptor MO1; Neutrophil adherence receptor; CD11b antigen M 0.02 mg


 

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