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Complement component C8 alpha chain (Complement component 8 subunit alpha)

 CO8A_HUMAN              Reviewed;         584 AA.
P07357; A2RUI4; A2RUI5; Q13668; Q9H130;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
30-AUG-2017, entry version 185.
RecName: Full=Complement component C8 alpha chain;
AltName: Full=Complement component 8 subunit alpha;
Flags: Precursor;
Name=C8A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=2820471; DOI=10.1021/bi00386a046;
Rao A.G., Howard O.M.Z., Ng S.C., Whitehead A.S., Colten H.R.,
Sodetz J.M.;
"Complementary DNA and derived amino acid sequence of the alpha
subunit of human complement protein C8: evidence for the existence of
a separate alpha subunit messenger RNA.";
Biochemistry 26:3556-3564(1987).
[2]
SEQUENCE REVISION TO 467-479.
Sodetz J.M.;
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=7759071; DOI=10.1007/BF00223862;
Michelotti G.A., Snider J.V., Sodetz J.M.;
"Genomic organization of human complement protein C8 alpha and further
examination of its linkage to C8 beta.";
Hum. Genet. 95:513-518(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-93.
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).
[6]
PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
PubMed=7440581;
Steckel E.W., York R.G., Monahan J.B., Sodetz J.M.;
"The eighth component of human complement. Purification and
physicochemical characterization of its unusual subunit structure.";
J. Biol. Chem. 255:11997-12005(1980).
[7]
GLYCOSYLATION AT TRP-44; TRP-542; TRP-545 AND TRP-548.
PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
"The four terminal components of the complement system are C-
mannosylated on multiple tryptophan residues.";
J. Biol. Chem. 274:32786-32794(1999).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-437.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-437.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-492, AND FUNCTION.
PubMed=17872444; DOI=10.1126/science.1147103;
Hadders M.A., Beringer D.X., Gros P.;
"Structure of C8alpha-MACPF reveals mechanism of membrane attack in
complement immune defense.";
Science 317:1552-1554(2007).
[12]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 133-492 IN COMPLEX WITH C8G,
AND INTERCHAIN DISULFIDE BOND.
PubMed=18440555; DOI=10.1016/j.jmb.2008.03.061;
Slade D.J., Lovelace L.L., Chruszcz M., Minor W., Lebioda L.,
Sodetz J.M.;
"Crystal structure of the MACPF domain of human complement protein C8
alpha in complex with the C8 gamma subunit.";
J. Mol. Biol. 379:331-342(2008).
[13]
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 188-198 IN COMPLEX WITH C8G.
PubMed=17692377; DOI=10.1016/j.molimm.2007.06.359;
Lovelace L.L., Chiswell B., Slade D.J., Sodetz J.M., Lebioda L.;
"Crystal structure of complement protein C8gamma in complex with a
peptide containing the C8gamma binding site on C8alpha: implications
for C8gamma ligand binding.";
Mol. Immunol. 45:750-756(2008).
[14]
VARIANT C8A*B LYS-93.
PubMed=7649542; DOI=10.1007/BF00210407;
Zhang L., Rittner C., Sodetz J.M., Schneider P.M., Kaufmann T.;
"The eighth component of human complement: molecular basis of C8A
(C81) polymorphism.";
Hum. Genet. 96:281-284(1995).
-!- FUNCTION: Constituent of the membrane attack complex (MAC) that
plays a key role in the innate and adaptive immune response by
forming pores in the plasma membrane of target cells. C8A inserts
into the target membrane, but does not form pores by itself.
{ECO:0000269|PubMed:17872444, ECO:0000269|PubMed:7440581}.
-!- SUBUNIT: Heterotrimer of 3 chains: alpha, beta and gamma. The
alpha and gamma chains are disulfide bonded. Component of the
membrane attack complex (MAC). MAC assembly is initiated by
proteolytic cleavage of C5 into C5a and C5b. C5b sequentially
binds C6, C7, C8 and multiple copies of the pore-forming subunit
C9. {ECO:0000269|PubMed:17692377, ECO:0000269|PubMed:18440555,
ECO:0000269|PubMed:7440581}.
-!- SUBCELLULAR LOCATION: Secreted. Cell membrane; Multi-pass membrane
protein. Note=Secreted as soluble protein. Inserts into the cell
membrane of target cells.
-!- DISEASE: Complement component 8 deficiency, 1 (C8D1) [MIM:613790]:
A rare defect of the complement classical pathway associated with
susceptibility to severe recurrent infections, predominantly by
Neisseria gonorrhoeae or Neisseria meningitidis. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
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EMBL; M16974; AAA52200.1; -; mRNA.
EMBL; U08006; AAA82124.1; -; Genomic_DNA.
EMBL; U07996; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U07997; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U07998; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U07999; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U08000; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U08001; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U08002; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U08003; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U08004; AAA82124.1; JOINED; Genomic_DNA.
EMBL; U08005; AAA82124.1; JOINED; Genomic_DNA.
EMBL; AL121998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC132911; AAI32912.1; -; mRNA.
EMBL; BC132913; AAI32914.1; -; mRNA.
CCDS; CCDS606.1; -.
PIR; I37213; C8HUA.
RefSeq; NP_000553.1; NM_000562.2.
UniGene; Hs.93210; -.
PDB; 2QOS; X-ray; 1.81 A; A=188-198.
PDB; 2QQH; X-ray; 2.50 A; A=133-366, A=410-492.
PDB; 2RD7; X-ray; 2.15 A; A=133-492.
PDB; 3OJY; X-ray; 2.51 A; A=31-584.
PDBsum; 2QOS; -.
PDBsum; 2QQH; -.
PDBsum; 2RD7; -.
PDBsum; 3OJY; -.
ProteinModelPortal; P07357; -.
SMR; P07357; -.
BioGrid; 107192; 13.
DIP; DIP-1125N; -.
STRING; 9606.ENSP00000354458; -.
TCDB; 1.C.39.3.1; the membrane attack complex/perforin (macpf) family.
iPTMnet; P07357; -.
PhosphoSitePlus; P07357; -.
BioMuta; C8A; -.
DMDM; 729167; -.
MaxQB; P07357; -.
PaxDb; P07357; -.
PeptideAtlas; P07357; -.
PRIDE; P07357; -.
DNASU; 731; -.
Ensembl; ENST00000361249; ENSP00000354458; ENSG00000157131.
GeneID; 731; -.
KEGG; hsa:731; -.
UCSC; uc001cyo.3; human.
CTD; 731; -.
DisGeNET; 731; -.
GeneCards; C8A; -.
HGNC; HGNC:1352; C8A.
MalaCards; C8A; -.
MIM; 120950; gene.
MIM; 613790; phenotype.
neXtProt; NX_P07357; -.
OpenTargets; ENSG00000157131; -.
Orphanet; 169150; Immunodeficiency due to a late component of complements deficiency.
PharmGKB; PA25951; -.
eggNOG; ENOG410IE8U; Eukaryota.
eggNOG; ENOG410Y5MF; LUCA.
GeneTree; ENSGT00550000074478; -.
HOGENOM; HOG000231146; -.
HOVERGEN; HBG005368; -.
InParanoid; P07357; -.
KO; K03997; -.
OMA; ACRCGPC; -.
OrthoDB; EOG091G07LK; -.
PhylomeDB; P07357; -.
TreeFam; TF330498; -.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-977606; Regulation of Complement cascade.
ChiTaRS; C8A; human.
EvolutionaryTrace; P07357; -.
GenomeRNAi; 731; -.
PRO; PR:P07357; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000157131; -.
CleanEx; HS_C8A; -.
Genevisible; P07357; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
GO; GO:0001848; F:complement binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0006956; P:complement activation; IDA:MGI.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
Gene3D; 2.20.100.10; -; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR001862; MAC_perforin.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR000884; TSP1_rpt.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF01823; MACPF; 1.
Pfam; PF00090; TSP_1; 1.
PRINTS; PR00764; COMPLEMENTC9.
SMART; SM00192; LDLa; 1.
SMART; SM00457; MACPF; 1.
SMART; SM00209; TSP1; 2.
SUPFAM; SSF57184; SSF57184; 3.
SUPFAM; SSF82895; SSF82895; 2.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
PROSITE; PS50092; TSP1; 2.
1: Evidence at protein level;
3D-structure; Cell membrane; Cleavage on pair of basic residues;
Complement alternate pathway; Complement pathway; Complete proteome;
Cytolysis; Direct protein sequencing; Disulfide bond; EGF-like domain;
Glycoprotein; Immunity; Innate immunity; Membrane;
Membrane attack complex; Polymorphism; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane beta strand.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 30 {ECO:0000255}.
/FTId=PRO_0000023585.
CHAIN 31 584 Complement component C8 alpha chain.
/FTId=PRO_0000023586.
DOMAIN 38 91 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 94 132 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 135 498 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 499 529 EGF-like.
DOMAIN 539 583 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
SITE 43 43 Not glycosylated.
CARBOHYD 44 44 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 542 542 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 545 545 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 548 548 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
DISULFID 39 74 {ECO:0000250}.
DISULFID 50 53 {ECO:0000250}.
DISULFID 84 90 {ECO:0000250}.
DISULFID 96 108 {ECO:0000250}.
DISULFID 102 121 {ECO:0000250}.
DISULFID 115 130 {ECO:0000250}.
DISULFID 140 177
DISULFID 194 194 Interchain (with C-60 in C8-gamma chain).
DISULFID 375 399
VARIANT 93 93 Q -> K (in allele C8A*B; dbSNP:rs652785).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7649542}.
/FTId=VAR_011889.
VARIANT 407 407 T -> I (in dbSNP:rs706479).
/FTId=VAR_011890.
VARIANT 458 458 D -> N (in dbSNP:rs17114555).
/FTId=VAR_033800.
VARIANT 485 485 R -> L (in dbSNP:rs1620075).
/FTId=VAR_011891.
VARIANT 561 561 E -> Q (in dbSNP:rs1342440).
/FTId=VAR_011892.
VARIANT 575 575 P -> L (in dbSNP:rs17300936).
/FTId=VAR_033801.
CONFLICT 575 575 P -> S (in Ref. 3; AAA82124).
{ECO:0000305}.
TURN 52 54 {ECO:0000244|PDB:3OJY}.
STRAND 56 60 {ECO:0000244|PDB:3OJY}.
STRAND 63 65 {ECO:0000244|PDB:3OJY}.
STRAND 78 83 {ECO:0000244|PDB:3OJY}.
STRAND 97 101 {ECO:0000244|PDB:3OJY}.
STRAND 103 105 {ECO:0000244|PDB:3OJY}.
HELIX 111 113 {ECO:0000244|PDB:3OJY}.
STRAND 116 118 {ECO:0000244|PDB:3OJY}.
STRAND 121 123 {ECO:0000244|PDB:3OJY}.
STRAND 127 129 {ECO:0000244|PDB:3OJY}.
STRAND 140 143 {ECO:0000244|PDB:2QQH}.
HELIX 149 152 {ECO:0000244|PDB:2RD7}.
STRAND 154 157 {ECO:0000244|PDB:2RD7}.
TURN 158 161 {ECO:0000244|PDB:2RD7}.
STRAND 162 168 {ECO:0000244|PDB:2RD7}.
STRAND 179 182 {ECO:0000244|PDB:2RD7}.
TURN 183 186 {ECO:0000244|PDB:2QQH}.
STRAND 189 191 {ECO:0000244|PDB:2QOS}.
TURN 192 195 {ECO:0000244|PDB:2QOS}.
STRAND 196 198 {ECO:0000244|PDB:2QOS}.
HELIX 201 203 {ECO:0000244|PDB:3OJY}.
STRAND 204 207 {ECO:0000244|PDB:2RD7}.
STRAND 212 217 {ECO:0000244|PDB:2RD7}.
STRAND 226 232 {ECO:0000244|PDB:2RD7}.
HELIX 233 243 {ECO:0000244|PDB:2RD7}.
STRAND 246 252 {ECO:0000244|PDB:2RD7}.
STRAND 260 266 {ECO:0000244|PDB:2RD7}.
HELIX 273 280 {ECO:0000244|PDB:2RD7}.
STRAND 287 303 {ECO:0000244|PDB:2RD7}.
STRAND 305 308 {ECO:0000244|PDB:2RD7}.
HELIX 312 319 {ECO:0000244|PDB:2RD7}.
HELIX 327 337 {ECO:0000244|PDB:2RD7}.
STRAND 339 358 {ECO:0000244|PDB:2RD7}.
HELIX 359 365 {ECO:0000244|PDB:2RD7}.
HELIX 369 379 {ECO:0000244|PDB:2RD7}.
HELIX 398 402 {ECO:0000244|PDB:2RD7}.
HELIX 408 413 {ECO:0000244|PDB:2RD7}.
STRAND 416 421 {ECO:0000244|PDB:2RD7}.
HELIX 443 449 {ECO:0000244|PDB:2RD7}.
TURN 450 452 {ECO:0000244|PDB:2RD7}.
STRAND 455 463 {ECO:0000244|PDB:2RD7}.
HELIX 464 470 {ECO:0000244|PDB:2RD7}.
HELIX 477 491 {ECO:0000244|PDB:2RD7}.
HELIX 496 498 {ECO:0000244|PDB:3OJY}.
TURN 503 505 {ECO:0000244|PDB:3OJY}.
STRAND 508 511 {ECO:0000244|PDB:3OJY}.
STRAND 514 517 {ECO:0000244|PDB:3OJY}.
STRAND 525 527 {ECO:0000244|PDB:3OJY}.
STRAND 552 554 {ECO:0000244|PDB:3OJY}.
STRAND 556 559 {ECO:0000244|PDB:3OJY}.
STRAND 578 582 {ECO:0000244|PDB:3OJY}.
SEQUENCE 584 AA; 65163 MW; 9F61DDA51D2F3BBA CRC64;
MFAVVFFILS LMTCQPGVTA QEKVNQRVRR AATPAAVTCQ LSNWSEWTDC FPCQDKKYRH
RSLLQPNKFG GTICSGDIWD QASCSSSTTC VRQAQCGQDF QCKETGRCLK RHLVCNGDQD
CLDGSDEDDC EDVRAIDEDC SQYEPIPGSQ KAALGYNILT QEDAQSVYDA SYYGGQCETV
YNGEWRELRY DSTCERLYYG DDEKYFRKPY NFLKYHFEAL ADTGISSEFY DNANDLLSKV
KKDKSDSFGV TIGIGPAGSP LLVGVGVSHS QDTSFLNELN KYNEKKFIFT RIFTKVQTAH
FKMRKDDIML DEGMLQSLME LPDQYNYGMY AKFINDYGTH YITSGSMGGI YEYILVIDKA
KMESLGITSR DITTCFGGSL GIQYEDKINV GGGLSGDHCK KFGGGKTERA RKAMAVEDII
SRVRGGSSGW SGGLAQNRST ITYRSWGRSL KYNPVVIDFE MQPIHEVLRH TSLGPLEAKR
QNLRRALDQY LMEFNACRCG PCFNNGVPIL EGTSCRCQCR LGSLGAACEQ TQTEGAKADG
SWSCWSSWSV CRAGIQERRR ECDNPAPQNG GASCPGRKVQ TQAC


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EH681 Complement component C8 alpha chain Elisa Kit 96T
CSB-EL004194HU Human Complement component C8 alpha chain(C8A) ELISA kit 96T
CSB-EL004194MO Mouse Complement component C8 alpha chain(C8A) ELISA kit 96T
CSB-EL004194RB Rabbit Complement component C8 alpha chain(C8A) ELISA kit SpeciesRabbit 96T
CSB-EL004194HU Human Complement component C8 alpha chain(C8A) ELISA kit SpeciesHuman 96T
CSB-EL004194MO Mouse Complement component C8 alpha chain(C8A) ELISA kit SpeciesMouse 96T
E1970h ELISA Kit FOR Complement component C8 alpha chain; organism: Human; gene name: C8A 96T
E1970m ELISA Kit FOR Complement component C8 alpha chain; organism: Mouse; gene name: C8a 96T
201-20-2849 ITGAX{integrin, alpha X (complement component 3 receptor 4 subunit)}rabbit.pAb 0.2ml


 

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