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Prothrombin (EC 3 4 21 5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]

 THRB_MOUSE              Reviewed;         618 AA.
P19221;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
29-SEP-2021, entry version 212.
RecName: Full=Prothrombin;
EC=3.4.21.5;
AltName: Full=Coagulation factor II;
Contains:
RecName: Full=Activation peptide fragment 1;
Contains:
RecName: Full=Activation peptide fragment 2;
Contains:
RecName: Full=Thrombin light chain;
Contains:
RecName: Full=Thrombin heavy chain;
Flags: Precursor;
Name=F2; Synonyms=Cf2;
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], AND GAMMA-CARBOXYGLUTAMATION AT GLU-50; GLU-51;
GLU-58; GLU-60; GLU-63; GLU-64; GLU-69; GLU-70; GLU-73 AND GLU-76.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=2222810; DOI=10.1089/dna.1990.9.487;
Friezner Degen S.J., Schaffer L.A., Jamison C.S., Grant S.G.,
Fitzgibbon J.J., Pai J.-A., Chapman V.M., Elliott R.W.;
"Characterization of the cDNA coding for mouse prothrombin and localization
of the gene on mouse chromosome 2.";
DNA Cell Biol. 9:487-498(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 384-618.
TISSUE=Liver;
PubMed=1557383; DOI=10.1073/pnas.89.7.2779;
Banfield D.K., Macgillivray R.T.;
"Partial characterization of vertebrate prothrombin cDNAs: amplification
and sequence analysis of the B chain of thrombin from nine different
species.";
Proc. Natl. Acad. Sci. U.S.A. 89:2779-2783(1992).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122; ASN-413 AND ASN-553.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-containing
tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
and Testis;
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).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 319-618, AND DISULFIDE BONDS.
PubMed=17428793; DOI=10.1074/jbc.m701323200;
Marino F., Chen Z.-W., Ergenekan C.E., Bush-Pelc L.A., Mathews F.S.,
Di Cera E.;
"Structural basis of Na+ activation mimicry in murine thrombin.";
J. Biol. Chem. 282:16355-16361(2007).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 317-618 OF MUTANT ALA-565 IN
COMPLEXES WITH PAR3/F2RL2 AND PAR4/F2RL3, AND MUTAGENESIS OF SER-565.
PubMed=17606903; DOI=10.1073/pnas.0704409104;
Bah A., Chen Z.-W., Bush-Pelc L.A., Mathews F.S., Di Cera E.;
"Crystal structures of murine thrombin in complex with the extracellular
fragments of murine protease-activated receptors PAR3 and PAR4.";
Proc. Natl. Acad. Sci. U.S.A. 104:11603-11608(2007).
-!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts
fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in
complex with thrombomodulin, protein C. Functions in blood homeostasis,
inflammation and wound healing (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form
fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
-!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
-!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy
chain; disulfide-linked. Forms a heterodimer with SERPINA5 (By
similarity). {ECO:0000250}.
-!- PTM: The gamma-carboxyglutamyl residues, which bind calcium ions,
result from the carboxylation of glutamyl residues by a microsomal
enzyme, the vitamin K-dependent carboxylase. The modified residues are
necessary for the calcium-dependent interaction with a negatively
charged phospholipid surface, which is essential for the conversion of
prothrombin to thrombin. {ECO:0000269|PubMed:2222810}.
-!- MISCELLANEOUS: Prothrombin is activated on the surface of a
phospholipid membrane that binds the amino end of prothrombin and
factors Va and Xa in Ca-dependent interactions; factor Xa removes the
activation peptide and cleaves the remaining part into light and heavy
chains. The activation process starts slowly because factor V itself
has to be activated by the initial, small amounts of thrombin.
-!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment
(fragment 1) of the prothrombin, prior to its activation by factor Xa.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
---------------------------------------------------------------------------
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EMBL; X52308; CAA36548.1; -; mRNA.
EMBL; BC013662; AAH13662.1; -; mRNA.
EMBL; M81394; AAA40435.1; -; mRNA.
CCDS; CCDS16434.1; -.
PIR; A35827; A35827.
RefSeq; NP_034298.1; NM_010168.3.
PDB; 2OCV; X-ray; 2.20 A; A=319-346, B=361-618.
PDB; 2PUX; X-ray; 2.00 A; A=317-360, B=361-618.
PDB; 2PV9; X-ray; 3.50 A; A=317-360, B=361-618.
PDB; 3EDX; X-ray; 2.40 A; A/C/E=317-360, B/D/F=361-618.
PDB; 3HK3; X-ray; 1.94 A; A=317-360, B=361-618.
PDB; 3HK6; X-ray; 3.20 A; A/C=317-360, B/D=361-618.
PDB; 3HKI; X-ray; 2.20 A; A/D=317-360, B/E=361-618.
PDBsum; 2OCV; -.
PDBsum; 2PUX; -.
PDBsum; 2PV9; -.
PDBsum; 3EDX; -.
PDBsum; 3HK3; -.
PDBsum; 3HK6; -.
PDBsum; 3HKI; -.
SMR; P19221; -.
BioGRID; 199568; 9.
DIP; DIP-60968N; -.
IntAct; P19221; 5.
MINT; P19221; -.
STRING; 10090.ENSMUSP00000028681; -.
BindingDB; P19221; -.
ChEMBL; CHEMBL1075308; -.
MEROPS; S01.217; -.
GlyGen; P19221; 4 sites.
iPTMnet; P19221; -.
PhosphoSitePlus; P19221; -.
SwissPalm; P19221; -.
CPTAC; non-CPTAC-3432; -.
CPTAC; non-CPTAC-5620; -.
jPOST; P19221; -.
PaxDb; P19221; -.
PeptideAtlas; P19221; -.
PRIDE; P19221; -.
ProteomicsDB; 259185; -.
Antibodypedia; 857; 1158 antibodies.
DNASU; 14061; -.
Ensembl; ENSMUST00000028681; ENSMUSP00000028681; ENSMUSG00000027249.
GeneID; 14061; -.
KEGG; mmu:14061; -.
UCSC; uc008kwg.2; mouse.
CTD; 2147; -.
MGI; MGI:88380; F2.
VEuPathDB; HostDB:ENSMUSG00000027249; -.
eggNOG; ENOG502QTSX; Eukaryota.
GeneTree; ENSGT00940000154234; -.
HOGENOM; CLU_006842_19_4_1; -.
InParanoid; P19221; -.
OMA; VMIFRKS; -.
OrthoDB; 1314811at2759; -.
PhylomeDB; P19221; -.
TreeFam; TF327329; -.
Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
Reactome; R-MMU-416476; G alpha (q) signalling events.
Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation).
Reactome; R-MMU-977606; Regulation of Complement cascade.
BioGRID-ORCS; 14061; 1 hit in 48 CRISPR screens.
ChiTaRS; F2; mouse.
EvolutionaryTrace; P19221; -.
PRO; PR:P19221; -.
Proteomes; UP000000589; Chromosome 2.
RNAct; P19221; protein.
Bgee; ENSMUSG00000027249; Expressed in liver and 102 other tissues.
ExpressionAtlas; P19221; baseline and differential.
Genevisible; P19221; MM.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008201; F:heparin binding; ISO:MGI.
GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IMP:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0070053; F:thrombospondin receptor activity; ISO:MGI.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
GO; GO:0007596; P:blood coagulation; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
GO; GO:0051838; P:cytolysis by host of symbiont cells; ISO:MGI.
GO; GO:0042730; P:fibrinolysis; ISO:MGI.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:MGI.
GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; ISO:MGI.
GO; GO:0030168; P:platelet activation; IDA:MGI.
GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI.
GO; GO:0030307; P:positive regulation of cell growth; IGI:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:0090218; P:positive regulation of lipid kinase activity; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IGI:MGI.
GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
GO; GO:0008360; P:regulation of cell shape; IGI:MGI.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0009611; P:response to wounding; ISO:MGI.
GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISO:MGI.
CDD; cd00108; KR; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 2.40.20.10; -; 2.
Gene3D; 4.10.140.10; -; 1.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR003966; Prothrombin/thrombin.
InterPro; IPR018992; Thrombin_light_chain.
InterPro; IPR037111; Thrombin_light_chain_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24254:SF10; PTHR24254:SF10; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00051; Kringle; 2.
Pfam; PF09396; Thrombin_light; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001149; Thrombin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
PRINTS; PR01505; PROTHROMBIN.
SMART; SM00069; GLA; 1.
SMART; SM00130; KR; 2.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 2.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS00021; KRINGLE_1; 2.
PROSITE; PS50070; KRINGLE_2; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Disulfide bond;
Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; Kringle;
Protease; Reference proteome; Repeat; Serine protease; Signal; Zymogen.
SIGNAL 1..24
/evidence="ECO:0000255"
PROPEP 25..43
/id="PRO_0000028165"
CHAIN 44..618
/note="Prothrombin"
/id="PRO_0000028166"
PEPTIDE 44..200
/note="Activation peptide fragment 1"
/id="PRO_0000028167"
PEPTIDE 201..324
/note="Activation peptide fragment 2"
/id="PRO_0000028168"
CHAIN 325..360
/note="Thrombin light chain"
/id="PRO_0000028169"
CHAIN 361..618
/note="Thrombin heavy chain"
/id="PRO_0000028170"
DOMAIN 44..90
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 109..187
/note="Kringle 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
DOMAIN 215..292
/note="Kringle 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
DOMAIN 361..615
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
REGION 548..570
/note="High affinity receptor-binding region which is also
known as the TP508 peptide"
/evidence="ECO:0000250"
ACT_SITE 403
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 459
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 565
/note="Charge relay system"
/evidence="ECO:0000250"
SITE 200..201
/note="Cleavage; by thrombin"
SITE 324..325
/note="Cleavage; by factor Xa"
SITE 360..361
/note="Cleavage; by factor Xa"
MOD_RES 50
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 51
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 58
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 60
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 63
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 64
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 69
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 70
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 73
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
MOD_RES 76
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2222810"
CARBOHYD 122
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:17330941"
CARBOHYD 144
/note="N-linked (GlcNAc...) asparagine"
CARBOHYD 413
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:17330941"
CARBOHYD 553
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:17330941"
DISULFID 61..66
/evidence="ECO:0000250"
DISULFID 91..104
/evidence="ECO:0000250"
DISULFID 109..187
/evidence="ECO:0000250"
DISULFID 130..170
/evidence="ECO:0000250"
DISULFID 158..182
/evidence="ECO:0000250"
DISULFID 215..293
/evidence="ECO:0000250"
DISULFID 236..276
/evidence="ECO:0000250"
DISULFID 264..288
/evidence="ECO:0000250"
DISULFID 333..479
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00121,
ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463"
DISULFID 388..404
/evidence="ECO:0000269|PubMed:17428793"
DISULFID 533..547
/evidence="ECO:0000269|PubMed:17428793"
DISULFID 561..591
/evidence="ECO:0000269|PubMed:17428793"
MUTAGEN 565
/note="S->A: Loss of protease activity."
/evidence="ECO:0000269|PubMed:17606903"
HELIX 323..326
/evidence="ECO:0007829|PDB:2PUX"
TURN 331..334
/evidence="ECO:0007829|PDB:3HK3"
TURN 337..339
/evidence="ECO:0007829|PDB:3HK3"
HELIX 340..342
/evidence="ECO:0007829|PDB:3HK3"
HELIX 349..354
/evidence="ECO:0007829|PDB:3HK3"
STRAND 375..380
/evidence="ECO:0007829|PDB:3HK3"
TURN 381..384
/evidence="ECO:0007829|PDB:3HK3"
STRAND 385..400
/evidence="ECO:0007829|PDB:3HK3"
HELIX 402..404
/evidence="ECO:0007829|PDB:3HK3"
HELIX 408..410
/evidence="ECO:0007829|PDB:3HK3"
HELIX 416..418
/evidence="ECO:0007829|PDB:3HK3"
STRAND 419..424
/evidence="ECO:0007829|PDB:3HK3"
STRAND 427..430
/evidence="ECO:0007829|PDB:3HK3"
TURN 433..435
/evidence="ECO:0007829|PDB:3HK3"
STRAND 437..446
/evidence="ECO:0007829|PDB:3HK3"
TURN 452..454
/evidence="ECO:0007829|PDB:3HK3"
STRAND 461..467
/evidence="ECO:0007829|PDB:3HK3"
HELIX 483..489
/evidence="ECO:0007829|PDB:3HK3"
STRAND 495..500
/evidence="ECO:0007829|PDB:3HK3"
STRAND 504..507
/evidence="ECO:0007829|PDB:2PUX"
HELIX 512..515
/evidence="ECO:0007829|PDB:2PUX"
STRAND 521..527
/evidence="ECO:0007829|PDB:3HK3"
HELIX 530..535
/evidence="ECO:0007829|PDB:3HK3"
STRAND 545..548
/evidence="ECO:0007829|PDB:3HK3"
STRAND 554..556
/evidence="ECO:0007829|PDB:3EDX"
HELIX 562..564
/evidence="ECO:0007829|PDB:3HK3"
STRAND 568..572
/evidence="ECO:0007829|PDB:3HK3"
TURN 574..576
/evidence="ECO:0007829|PDB:3HK3"
STRAND 579..587
/evidence="ECO:0007829|PDB:3HK3"
HELIX 591..593
/evidence="ECO:0007829|PDB:3HK3"
STRAND 596..602
/evidence="ECO:0007829|PDB:3HK3"
HELIX 604..606
/evidence="ECO:0007829|PDB:3HK3"
HELIX 607..617
/evidence="ECO:0007829|PDB:3HK3"
SEQUENCE 618 AA; 70269 MW; B89F719AAFD601E0 CRC64;
MSHVRGLGLP GCLALAALVS LVHSQHVFLA PQQALSLLQR VRRANSGFLE ELRKGNLERE
CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET FMDCLEGRCA MDLGVNYLGT
VNVTHTGIQC QLWRSRYPHK PEINSTTHPG ADLKENFCRN PDSSTTGPWC YTTDPTVRRE
ECSVPVCGQE GRTTVVMTPR SGGSKDNLSP PLGQCLTERG RLYQGNLAVT TLGSPCLPWN
SLPAKTLSKY QDFDPEVKLV ENFCRNPDWD EEGAWCYVAG QPGDFEYCNL NYCEEAVGEE
NYDVDESIAG RTTDAEFHTF FNEKTFGLGE ADCGLRPLFE KKSLKDTTEK ELLDSYIDGR
IVEGWDAEKG IAPWQVMLFR KSPQELLCGA SLISDRWVLT AAHCILYPPW DKNFTENDLL
VRIGKHSRTR YERNVEKISM LEKIYVHPRY NWRENLDRDI ALLKLKKPVP FSDYIHPVCL
PDKQTVTSLL RAGYKGRVTG WGNLRETWTT NINEIQPSVL QVVNLPIVER PVCKASTRIR
ITDNMFCAGF KVNDTKRGDA CEGDSGGPFV MKSPFNNRWY QMGIVSWGEG CDRKGKYGFY
THVFRLKRWI QKVIDQFG


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bs-10388R-Cy5.5 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, Cy5.5 Conjugated 100ul
bs-10387R-Cy5.5 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, Cy5.5 Conjugated 100ul
bs-10387R-HRP Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, HRP Conjugated 100ul
bs-10388R-Cy7 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, Cy7 Conjugated 100ul
bs-10387R-Cy7 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, Cy7 Conjugated 100ul
bs-10387R-Cy3 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, Cy3 Conjugated 100ul
bs-10388R-Cy3 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, Cy3 Conjugated 100ul
bs-10388R-HRP Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, HRP Conjugated 100ul
bs-10387R-Cy5 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, Cy5 Conjugated 100ul
bs-10388R-A594 Thrombin Activation peptide fragment 2 Antibody, ALEXA FLUOR 594 Conjugated 100ul
bs-10387R-A594 Thrombin Activation peptide fragment 1 Antibody, ALEXA FLUOR 594 Conjugated 100ul
bs-10388R-Cy5 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, Cy5 Conjugated 100ul
bs-10388R-A488 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-10388R-A647 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-10387R-A488 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-10388R-A555 Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-10387R-A555 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-10387R-A647 Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-10388R-Biotin Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, Biotin Conjugated 100ul
bs-10387R-Biotin Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, Biotin Conjugated 100ul
bs-10388R-FITC Rabbit Anti-Thrombin Activation peptide fragment 2 Polyclonal Antibody, FITC Conjugated 100ul
bs-10387R-FITC Rabbit Anti-Thrombin Activation peptide fragment 1 Polyclonal Antibody, FITC Conjugated 100ul
R1391T Rat IgG Fab Fragment (Heavy and Light chain) 1 mg
Pathways :
WP272: Blood Clotting Cascade
WP1614: 1- and 2-Methylnaphthalene degradation
WP545: Complement Activation, Classical Pathway
WP1001: Peptide GPCRs
WP977: Complement Activation, Classical Pathway
WP200: Complement Activation, Classical Pathway
WP1647: Fatty acid biosynthesis
WP59: Electron Transport Chain
WP1673: Naphthalene and anthracene degradation
WP772: Electron Transport Chain
WP1117: Peptide GPCRs
WP234: Peptide GPCRs
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1823: GP1b-IX-V activation signalling
WP1882: Platelet Activation
WP884: Electron Transport Chain
WP131: Peptide GPCRs
WP1502: Mitochondrial biogenesis
WP542: Electron Transport Chain
WP1929: Thrombin signalling through proteinase activated receptors (PARs)
WP1996: Linoleate Biosynthesis
WP1633: Bisphenol A degradation
WP1665: Limonene and pinene degradation
WP771: Peptide GPCRs
WP111: Electron Transport Chain

Related Genes :
[F2] Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]
[PROC] Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]
[] Venom prothrombin activator pseutarin-C catalytic subunit (PCCS) (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10 FX] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Virus-activating protease) (VAP) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[PLG] Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B]
[F7 Cf7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F2RL1 GPR11 PAR2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]
[F11] Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain]
[F12] Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)]
[F9] Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain]
[F8 F8C] Coagulation factor VIII (Antihemophilic factor) (AHF) (Procoagulant component) [Cleaved into: Factor VIIIa heavy chain, 200 kDa isoform; Factor VIIIa heavy chain, 92 kDa isoform; Factor VIII B chain; Factor VIIIa light chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B heavy chain]
[F2 ORTSPA_R05543] Activation peptide fragment 1 (EC 3.4.21.5) (Activation peptide fragment 2) (Coagulation factor II) (Prothrombin) (Thrombin heavy chain) (Thrombin light chain) (Fragment)
[F2 EULNIG_R03319] Activation peptide fragment 1 (EC 3.4.21.5) (Activation peptide fragment 2) (Coagulation factor II) (Prothrombin) (Thrombin heavy chain) (Thrombin light chain) (Fragment)
[F10 TrFX] Coagulation factor X (EC 3.4.21.6) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[HABP2 HGFAL PHBP] Hyaluronan-binding protein 2 (EC 3.4.21.-) (Factor VII-activating protease) (Factor seven-activating protease) (FSAP) (Hepatocyte growth factor activator-like protein) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form]
[F13A1 F13A] Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A chain)
[F2rl1 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (Thrombin receptor-like 1)
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F2rl1 Gpcr11 Gpr11 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1)
[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]

Bibliography :
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