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Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]

 FIBA_RAT                Reviewed;         782 AA.
P06399;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 3.
23-MAY-2018, entry version 146.
RecName: Full=Fibrinogen alpha chain;
Contains:
RecName: Full=Fibrinopeptide A;
Contains:
RecName: Full=Fibrinogen alpha chain;
Flags: Precursor;
Name=Fga;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8595905; DOI=10.1006/geno.1995.0010;
Fu Y., Cao Y., Hertzberg K.M., Grieninger G.;
"Fibrinogen alpha genes: conservation of bipartite transcripts and
carboxy-terminal-extended alpha subunits in vertebrates.";
Genomics 30:71-76(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=4046033; DOI=10.1016/0022-2836(85)90179-2;
Crabtree G.R., Comeau C.M., Fowlkes D.M., Fornace A.J. Jr.,
Malley J.D., Kant J.A.;
"Evolution and structure of the fibrinogen genes. Random insertion of
introns or selective loss?";
J. Mol. Biol. 185:1-19(1985).
[3]
PROTEIN SEQUENCE OF 20-36.
Blombaeck B., Blombaeck M., Grondahl N.J.;
"Studies on fibrinopeptides from mammals.";
Acta Chem. Scand. 19:1789-1791(1965).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 458-550 (ISOFORM 2).
STRAIN=Wistar; TISSUE=Liver;
PubMed=3817019; DOI=10.1016/0014-4827(87)90223-0;
Sobczak J., Lotti A.-M., Taroux P., Duguet M.;
"Molecular cloning of mRNA sequences transiently induced during rat
liver regeneration.";
Exp. Cell Res. 169:47-56(1987).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; SER-326; SER-470
AND SER-526, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Cleaved by the protease thrombin to yield monomers
which, together with fibrinogen beta (FGB) and fibrinogen gamma
(FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a
major function in hemostasis as one of the primary components of
blood clots. In addition, functions during the early stages of
wound repair to stabilize the lesion and guide cell migration
during re-epithelialization. Was originally thought to be
essential for platelet aggregation, based on in vitro studies
using anticoagulated blood. However, subsequent studies have shown
that it is not absolutely required for thrombus formation in vivo.
Enhances expression of SELP in activated platelets via an ITGB3-
dependent pathway. Maternal fibrinogen is essential for successful
pregnancy. Fibrin deposition is also associated with infection,
where it protects against IFNG-mediated hemorrhage. May also
facilitate the immune response via both innate and T-cell mediated
pathways. {ECO:0000250|UniProtKB:E9PV24}.
-!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3
non-identical chains (alpha, beta and gamma). The 2 heterotrimers
are in head to head conformation with the N-termini in a small
central domain (By similarity). {ECO:0000250|UniProtKB:P02671}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02671}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha-E;
IsoId=P06399-1; Sequence=Displayed;
Name=2; Synonyms=Alpha;
IsoId=P06399-2; Sequence=VSP_001533, VSP_001534;
Note=Major isoform.;
-!- DOMAIN: A long coiled coil structure formed by 3 polypeptide
chains connects the central nodule to the C-terminal domains
(distal nodules). The long C-terminal ends of the alpha chains
fold back, contributing a fourth strand to the coiled coil
structure. {ECO:0000250|UniProtKB:P02671}.
-!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin,
which cleaves fibrinopeptides A and B from alpha and beta chains,
and thus exposes the N-terminal polymerization sites responsible
for the formation of the soft clot. The soft clot is converted
into the hard clot by factor XIIIA which catalyzes the epsilon-
(gamma-glutamyl)lysine cross-linking between gamma chains
(stronger) and between alpha chains (weaker) of different
monomers.
-!- PTM: Forms F13A-mediated cross-links between a glutamine and the
epsilon-amino group of a lysine residue, forming fibronectin-
fibrinogen heteropolymers.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P02671}.
-----------------------------------------------------------------------
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EMBL; X86561; CAA60264.1; -; Genomic_DNA.
EMBL; X86561; CAA60263.1; -; Genomic_DNA.
EMBL; M35601; AAA41158.1; -; mRNA.
PIR; I53408; I53408.
UniGene; Rn.98846; -.
ProteinModelPortal; P06399; -.
SMR; P06399; -.
STRING; 10116.ENSRNOP00000060007; -.
iPTMnet; P06399; -.
PhosphoSitePlus; P06399; -.
PaxDb; P06399; -.
PeptideAtlas; P06399; -.
PRIDE; P06399; -.
UCSC; RGD:2603; rat. [P06399-1]
RGD; 2603; Fga.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
HOGENOM; HOG000285947; -.
HOVERGEN; HBG005668; -.
InParanoid; P06399; -.
PhylomeDB; P06399; -.
PMAP-CutDB; P06399; -.
PRO; PR:P06399; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0072562; C:blood microparticle; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; TAS:RGD.
GO; GO:1990643; P:cellular response to granulocyte colony-stimulating factor; IEP:RGD.
GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0044468; P:envenomation resulting in modulation of blood coagulation in other organism; IEP:RGD.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0030168; P:platelet activation; IEA:InterPro.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:RGD.
GO; GO:0051258; P:protein polymerization; IEA:InterPro.
GO; GO:0046898; P:response to cycloheximide; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0033595; P:response to genistein; IEP:RGD.
GO; GO:0060416; P:response to growth hormone; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0043278; P:response to morphine; IEP:RGD.
GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0010165; P:response to X-ray; IEP:RGD.
CDD; cd00087; FReD; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR021996; Fibrinogen_aC.
InterPro; IPR037579; Fibrinogen_alpha.
InterPro; IPR020837; Fibrinogen_CS.
PANTHER; PTHR19143:SF232; PTHR19143:SF232; 2.
Pfam; PF08702; Fib_alpha; 1.
Pfam; PF12160; Fibrinogen_aC; 1.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SMART; SM01212; Fib_alpha; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00514; FIBRINOGEN_C_1; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Blood coagulation; Calcium;
Coiled coil; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemostasis; Hydroxylation; Immunity;
Innate immunity; Metal-binding; Phosphoprotein; Reference proteome;
Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|Ref.3}.
PEPTIDE 20 36 Fibrinopeptide A.
/FTId=PRO_0000009039.
CHAIN 37 782 Fibrinogen alpha chain.
/FTId=PRO_0000009038.
DOMAIN 539 780 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
COILED 68 547 {ECO:0000250|UniProtKB:P02671}.
METAL 707 707 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 709 709 Calcium. {ECO:0000250|UniProtKB:P02671}.
METAL 711 711 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
METAL 713 713 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P02671}.
SITE 36 37 Cleavage; by thrombin; to release
fibrinopeptide A.
SITE 101 102 Cleavage; by plasmin; to break down
fibrin clots.
{ECO:0000250|UniProtKB:P02671}.
SITE 122 123 Cleavage; by hementin; to prevent blood
coagulation.
{ECO:0000250|UniProtKB:P02671}.
SITE 124 125 Cleavage; by plasmin; to break down
fibrin clots.
{ECO:0000250|UniProtKB:P02671}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 499 499 4-hydroxyproline; by P4HA1.
{ECO:0000250|UniProtKB:P02671}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 48 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00739}.
DISULFID 56 56 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 65 65 Interchain (with C-49 in gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 69 69 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 181 181 Interchain (with C-165 in gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 185 185 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 404 434 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 715 728 {ECO:0000250|UniProtKB:P02671}.
VAR_SEQ 547 550 DCDD -> GIHA (in isoform 2).
{ECO:0000303|PubMed:3817019}.
/FTId=VSP_001533.
VAR_SEQ 551 782 Missing (in isoform 2).
{ECO:0000303|PubMed:3817019}.
/FTId=VSP_001534.
CONFLICT 30 34 EAGGD -> DEGAG (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 140 140 Q -> E (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 212 212 D -> E (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 270 276 ASRGDLP -> LREEIYQ (in Ref. 2).
{ECO:0000305}.
CONFLICT 473 473 S -> K (in Ref. 4; AAA41158).
{ECO:0000305}.
SEQUENCE 782 AA; 86686 MW; 744834DAE76D34C2 CRC64;
MLSLRVACLI LSLASTVWTA DTGTTSEFIE AGGDIRGPRI VERQPSQCKE TDWPFCSDED
WNHKCPSGCR MKGLIDEANQ DFTNRINKLK NSLFDFQKNN KDSNSLTRNI MEYLRGDFAN
ANNFDNTFGQ VSEDLRRRIQ ILKRKVIEKA QQIQVLQKDV RDQLIDMKRL EVDIDIKIRS
CKGSCSRSVS REINLKDYEG QQKQLEQVIA KDLLPAKDRQ YLPAIKMSPV PDLVPGSFKS
QLQEGPPEWK ALTEMRQMRM ELERPGKDGA SRGDLPGDSR GDSATRGPGS KIENPMTPGH
GGSGYWRPGS SGSGSDGNWG SGTTGSDDTG TWGAGSSRPS SGSGNLKPSN PDWGEFSEFG
GSSSPATRKE YHTGKLVTSK GDKELLIGNE KVTSTGTSTT RRSCSKTITK TVLGNDGHRE
VVKEVVTSDD GSDCGDGMDL GLTHSFSGRL DELSRMHPEL GSFYDSRFGS LTSNFKEFGS
KTSDSDIFTD IENPSSHVPE FSSSSKTSTV RKQVTKSYKM ADEAASEAHQ EGDTRTTKRG
RARTMRDCDD VLQTHPSGAQ NGIFSIKLPG SSKIFSVYCD QETSLGGWLL IQQRMDGSLN
FNRTWQDYKR GFGSLNDKGE GEFWLGNDYL HLLTLRGSVL RVELEDWAGK EAYAEYHFRV
GSEAEGYALQ VSSYQGTAGD ALMEGSVEEG TEYTSHSNMQ FSTFDRDADQ WEENCAEVYG
GGWWYNSCQA ANLNGIYYPG GTYDPRNNSP YEIENGVLWV PFRGADYSLW AVRMKIRPLV
GQ


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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1002: Electron Transport Chain
WP1003: Ovarian Infertility Genes
WP1047: TNF-alpha NF-kB Signaling Pathway
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1120: Ovarian Infertility Genes
WP1163: TNF-alpha NF-kB Signaling Pathway
WP1209: EBV LMP1 signaling
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1339: Electron Transport Chain
WP1340: Ovarian Infertility Genes
WP1369: TNF-alpha NF-kB Signaling Pathway
WP1434: Osteopontin Signaling
WP1487: TNF-alpha and mucus production in lung epythelium
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1571: EBV LMP1 signaling
WP1584: Type II diabetes mellitus
WP1618: alpha-Linolenic acid metabolism
WP1626: Benzoate degradation via CoA ligation
WP1633: Bisphenol A degradation
WP1647: Fatty acid biosynthesis

Related Genes :
[FGA] Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]
[Fga] Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]
[Fga] Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]
[FGB] Fibrinogen beta chain [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain]
[ITGA2B GP2B ITGAB] Integrin alpha-IIb (GPalpha IIb) (GPIIb) (Platelet membrane glycoprotein IIb) (CD antigen CD41) [Cleaved into: Integrin alpha-IIb heavy chain; Integrin alpha-IIb light chain, form 1; Integrin alpha-IIb light chain, form 2]
[FGG PRO2061] Fibrinogen gamma chain
[FCN1 FCNM] Ficolin-1 (Collagen/fibrinogen domain-containing protein 1) (Ficolin-A) (Ficolin-alpha) (M-ficolin)
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase, beta-subunit (RT-beta); Reverse transcriptase, alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; p3; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[FCN3 FCNH HAKA1] Ficolin-3 (Collagen/fibrinogen domain-containing lectin 3 p35) (Collagen/fibrinogen domain-containing protein 3) (Hakata antigen)
[ITGAV MSK8 VNRA VTNR] Integrin alpha-V (Vitronectin receptor) (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]
[Itgav] Integrin alpha-V (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; p3; Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[C3 CPAMD1] Complement C3 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 (HSE-MSF) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[HADHA HADH] Trifunctional enzyme subunit alpha, mitochondrial (78 kDa gastrin-binding protein) (TP-alpha) [Includes: Long-chain enoyl-CoA hydratase (EC 4.2.1.17); Long chain 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211)]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc) (Neutrophil chemotactic factor-2) (ENCF-2); Complement C3 alpha chain; C3a anaphylatoxin (Neutrophil chemotactic factor-1) (ENCF-1); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; C3-beta-c (C3bc); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[c3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] (Fragment)
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[TUBA1A TUBA3] Tubulin alpha-1A chain (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
[ITGAM CD11B CR3A] Integrin alpha-M (CD11 antigen-like family member B) (CR-3 alpha chain) (Cell surface glycoprotein MAC-1 subunit alpha) (Leukocyte adhesion receptor MO1) (Neutrophil adherence receptor) (CD antigen CD11b)
[Tuba1a Tuba1] Tubulin alpha-1A chain (Alpha-tubulin 1) (Alpha-tubulin isotype M-alpha-1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
[C4A CO4 CPAMD2] Complement C4-A (Acidic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2) [Cleaved into: Complement C4 beta chain; Complement C4-A alpha chain; C4a anaphylatoxin; C4b-A; C4d-A; Complement C4 gamma chain]
[ITIH4 IHRP ITIHL1 PK120 PRO1851] Inter-alpha-trypsin inhibitor heavy chain H4 (ITI heavy chain H4) (ITI-HC4) (Inter-alpha-inhibitor heavy chain 4) (Inter-alpha-trypsin inhibitor family heavy chain-related protein) (IHRP) (Plasma kallikrein sensitive glycoprotein 120) (Gp120) (PK-120) [Cleaved into: 70 kDa inter-alpha-trypsin inhibitor heavy chain H4; 35 kDa inter-alpha-trypsin inhibitor heavy chain H4]
[Tuba3a Tuba3; Tuba3b Tuba7] Tubulin alpha-3 chain (Alpha-tubulin 3/7) (Alpha-tubulin isotype M-alpha-3/7) (Tubulin alpha-3/alpha-7 chain) [Cleaved into: Detyrosinated tubulin alpha-3 chain]
[Tuba1a Tuba1] Tubulin alpha-1A chain (Alpha-tubulin 1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
[AHSG FETUA PRO2743] Alpha-2-HS-glycoprotein (Alpha-2-Z-globulin) (Ba-alpha-2-glycoprotein) (Fetuin-A) [Cleaved into: Alpha-2-HS-glycoprotein chain A; Alpha-2-HS-glycoprotein chain B]
[] Phospholipase A2 homolog crotoxin acid subunit CA (CTX subunit CA) (Crotapotin) [Cleaved into: Crotoxin chain alpha CA1, CA2 and CA4; Crotoxin chain alpha CA3; Crotoxin chain beta CA2, CA3 and CA4; Crotoxin chain beta CA1; Crotoxin chain gamma (Analgesic peptide) (Crotalphine)]

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