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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.
12-SEP-2018, entry version 193.
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: Selective cleavage of Arg-|-Gly bonds in
fibrinogen to form fibrin and release fibrinopeptides A and B.
-!- 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.
UniGene; Mm.89048; -.
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; -.
ProteinModelPortal; P19221; -.
SMR; P19221; -.
DIP; DIP-60968N; -.
IntAct; P19221; 6.
MINT; P19221; -.
STRING; 10090.ENSMUSP00000028681; -.
BindingDB; P19221; -.
ChEMBL; CHEMBL1075308; -.
MEROPS; S01.217; -.
iPTMnet; P19221; -.
PhosphoSitePlus; P19221; -.
SwissPalm; P19221; -.
PaxDb; P19221; -.
PeptideAtlas; P19221; -.
PRIDE; P19221; -.
Ensembl; ENSMUST00000028681; ENSMUSP00000028681; ENSMUSG00000027249.
GeneID; 14061; -.
KEGG; mmu:14061; -.
UCSC; uc008kwg.2; mouse.
CTD; 2147; -.
MGI; MGI:88380; F2.
eggNOG; ENOG410IKPN; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOGENOM; HOG000251824; -.
HOVERGEN; HBG108381; -.
InParanoid; P19221; -.
KO; K01313; -.
OMA; HPVCLPD; -.
OrthoDB; EOG091G0AH5; -.
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-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
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.
ChiTaRS; F2; mouse.
EvolutionaryTrace; P19221; -.
PMAP-CutDB; P19221; -.
PRO; PR:P19221; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027249; Expressed in 70 organ(s), highest expression level in liver.
CleanEx; MM_F2; -.
ExpressionAtlas; P19221; baseline and differential.
Genevisible; P19221; MM.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008047; F:enzyme activator activity; IDA:MGI.
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; IMP:MGI.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; IMP: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 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; 2.40.20.10; -; 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; 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; Complete proteome; Disulfide bond;
Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
Kringle; Protease; Reference proteome; Repeat; Serine protease;
Signal; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 43
/FTId=PRO_0000028165.
CHAIN 44 618 Prothrombin.
/FTId=PRO_0000028166.
PEPTIDE 44 200 Activation peptide fragment 1.
/FTId=PRO_0000028167.
PEPTIDE 201 324 Activation peptide fragment 2.
/FTId=PRO_0000028168.
CHAIN 325 360 Thrombin light chain.
/FTId=PRO_0000028169.
CHAIN 361 618 Thrombin heavy chain.
/FTId=PRO_0000028170.
DOMAIN 44 90 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 109 187 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 215 292 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 361 615 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 548 570 High affinity receptor-binding region
which is also known as the TP508 peptide.
{ECO:0000250}.
ACT_SITE 403 403 Charge relay system. {ECO:0000250}.
ACT_SITE 459 459 Charge relay system. {ECO:0000250}.
ACT_SITE 565 565 Charge relay system. {ECO:0000250}.
SITE 200 201 Cleavage; by thrombin.
SITE 324 325 Cleavage; by factor Xa.
SITE 360 361 Cleavage; by factor Xa.
MOD_RES 50 50 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 51 51 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 58 58 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 60 60 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 63 63 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 64 64 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 69 69 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 70 70 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 73 73 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
MOD_RES 76 76 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:2222810}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 553 553 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
DISULFID 61 66 {ECO:0000250}.
DISULFID 91 104 {ECO:0000250}.
DISULFID 109 187 {ECO:0000250}.
DISULFID 130 170 {ECO:0000250}.
DISULFID 158 182 {ECO:0000250}.
DISULFID 215 293 {ECO:0000250}.
DISULFID 236 276 {ECO:0000250}.
DISULFID 264 288 {ECO:0000250}.
DISULFID 333 479 Interchain (between light and heavy
chains). {ECO:0000255|PROSITE-
ProRule:PRU00121, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463}.
DISULFID 388 404 {ECO:0000269|PubMed:17428793}.
DISULFID 533 547 {ECO:0000269|PubMed:17428793}.
DISULFID 561 591 {ECO:0000269|PubMed:17428793}.
MUTAGEN 565 565 S->A: Loss of protease activity.
{ECO:0000269|PubMed:17606903}.
HELIX 323 326 {ECO:0000244|PDB:2PUX}.
TURN 331 334 {ECO:0000244|PDB:3HK3}.
TURN 337 339 {ECO:0000244|PDB:3HK3}.
HELIX 340 342 {ECO:0000244|PDB:3HK3}.
HELIX 349 354 {ECO:0000244|PDB:3HK3}.
STRAND 375 380 {ECO:0000244|PDB:3HK3}.
TURN 381 384 {ECO:0000244|PDB:3HK3}.
STRAND 385 400 {ECO:0000244|PDB:3HK3}.
HELIX 402 404 {ECO:0000244|PDB:3HK3}.
HELIX 408 410 {ECO:0000244|PDB:3HK3}.
HELIX 416 418 {ECO:0000244|PDB:3HK3}.
STRAND 419 424 {ECO:0000244|PDB:3HK3}.
STRAND 427 430 {ECO:0000244|PDB:3HK3}.
TURN 433 435 {ECO:0000244|PDB:3HK3}.
STRAND 437 446 {ECO:0000244|PDB:3HK3}.
TURN 452 454 {ECO:0000244|PDB:3HK3}.
STRAND 461 467 {ECO:0000244|PDB:3HK3}.
HELIX 483 489 {ECO:0000244|PDB:3HK3}.
STRAND 495 500 {ECO:0000244|PDB:3HK3}.
STRAND 504 507 {ECO:0000244|PDB:2PUX}.
HELIX 512 515 {ECO:0000244|PDB:2PUX}.
STRAND 521 527 {ECO:0000244|PDB:3HK3}.
HELIX 530 535 {ECO:0000244|PDB:3HK3}.
STRAND 545 548 {ECO:0000244|PDB:3HK3}.
STRAND 554 556 {ECO:0000244|PDB:3EDX}.
HELIX 562 564 {ECO:0000244|PDB:3HK3}.
STRAND 568 572 {ECO:0000244|PDB:3HK3}.
TURN 574 576 {ECO:0000244|PDB:3HK3}.
STRAND 579 587 {ECO:0000244|PDB:3HK3}.
HELIX 591 593 {ECO:0000244|PDB:3HK3}.
STRAND 596 602 {ECO:0000244|PDB:3HK3}.
HELIX 604 606 {ECO:0000244|PDB:3HK3}.
HELIX 607 617 {ECO:0000244|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-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


 

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