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Coagulation Factor II (F2)

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FII; TM; PT; Thrombin; Prothrombin; Pro-Thrombin; Activation peptide fragment 1; Activation peptide fragment 2

Coagulation Factor II (F2)
CCC A820
HGNC 3535
MGI 88380
PubMed 2607889
RGD 61996
UniProt P00734
Wiki Thrombin

Thrombin (activated Factor II [IIa]) also commonly called pro-thrombin is a coagulation protein in the blood stream that has many effects in the coagulation cascade. It is a serine protease (EC 3.4.21.5) that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. The Thrombin (prothrombin) gene is located on the eleventh chromosome (11p11-q12). The molecular weight of prothrombin is approximately 72000 gmol-1. The catalytic domain is released from prothrombin fragment 1.2 to create the active enzyme thrombin, which has a molecular weight of 36000 gmol-1.There are an estimated 30 people in the world that have been diagnosed with the congenital form of Factor II deficiency, which should not be confused with a mutation of prothrombin.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA820Hu01 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
RPA820Hu02 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
RPA820Hu03 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
NPA820Hu01 Native Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAA820Hu01 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC; ICC; IP.
MAA820Hu22 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Hu21 Monoclonal Antibody to Coagulation Factor II (F2) WB
MAA820Hu23 Monoclonal Antibody to Coagulation Factor II (F2) WB
MAA820Hu24 Monoclonal Antibody to Coagulation Factor II (F2) WB; ICC/IF
PAA820Hu02 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Hu25 Monoclonal Antibody to Coagulation Factor II (F2) WB
MAA820Hu27 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Hu29 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
Assay Kits SEA820Hu ELISA Kit for Coagulation Factor II (F2) Enzyme-linked immunosorbent assay for Antigen Detection.
SCA820Hu CLIA Kit for Coagulation Factor II (F2) Chemiluminescent immunoassay for Antigen Detection.
AEA820Hu ELISA Kit for Anti-Coagulation Factor II Antibody (Anti-F2) Enzyme-linked immunosorbent assay for Antibody Detection.

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA820Mu01 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
RPA820Mu03 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
RPA820Mu02 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
EPA820Mu61 Eukaryotic Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAA820Mu01 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC; ICC/IF
PAA820Mu02 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC; ICC/IF
PAA820Mu03 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC
LAA820Mu71 Biotin-Linked Polyclonal Antibody to Coagulation Factor II (F2) WB
LAA820Mu81 FITC-Linked Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC; ICC; IF.
MAA820Mu22 Monoclonal Antibody to Coagulation Factor II (F2) WB
MAA820Mu21 Monoclonal Antibody to Coagulation Factor II (F2) WB
PAA820Mu06 Polyclonal Antibody to Coagulation Factor II (F2) WB
Assay Kits SEA820Mu ELISA Kit for Coagulation Factor II (F2) Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Rattus norvegicus (Rat)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA820Ra01 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
RPA820Ra02 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
RPA820Ra03 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
APA820Ra02 Active Coagulation Factor II (F2) Cell culture; Activity Assays.
Antibodies PAA820Ra01 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC
PAA820Ra02 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC; ICC/IF
MAA820Ra22 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
LAA820Ra71 Biotin-Linked Polyclonal Antibody to Coagulation Factor II (F2) WB
LAA820Ra81 FITC-Linked Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC; ICC; IF.
PAA820Ra03 Polyclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Ra21 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Ra23 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Ra24 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Ra25 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Ra27 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC; ICC/IF
MAA820Ra29 Monoclonal Antibody to Coagulation Factor II (F2) WB; IHC
MAA820Ra26 Monoclonal Antibody to Coagulation Factor II (F2) ICC/IF
Assay Kits SEA820Ra ELISA Kit for Coagulation Factor II (F2) Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Sus scrofa; Porcine (Pig)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Coagulation Factor II (F2) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Coagulation Factor II (F2) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Coagulation Factor II (F2) Polyclonal Antibody Customized Service Offer
Assay Kits SEA820Po ELISA Kit for Coagulation Factor II (F2) Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Bos taurus; Bovine (Cattle)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA820Bo01 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
RPA820Bo02 Recombinant Coagulation Factor II (F2) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAA820Bo01 Polyclonal Antibody to Coagulation Factor II (F2) WB
Assay Kits SEA820Bo ELISA Kit for Coagulation Factor II (F2) Enzyme-linked immunosorbent assay for Antigen Detection.
  1. "Nucleotide sequence of the gene for human prothrombin."Biochemistry 26:6165-6177(1987) [PubMed] [Europe PMC] [Abstract]
  2. "Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 by Gly."Haemophilia 10:94-97(2004) [PubMed] [Europe PMC] [Abstract]
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs." Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  5. "Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin."Biochemistry 22:2087-2097(1983) [PubMed] [Europe PMC] [Abstract]
  6. "Isolation and partial characterization of crystal matrix protein as a potent inhibitor of calcium oxalate crystal aggregation: evidence of activation peptide of human prothrombin."Urol. Res. 22:45-50(1994) [PubMed] [Europe PMC] [Abstract]
  7. "Amino acid sequence of human prothrombin fragments 1 and 2."Proc. Natl. Acad. Sci. U.S.A. 74:1969-1972(1977) [PubMed] [Europe PMC] [Abstract]
  8. "Primary structure of human prethrombin 2 and alpha-thrombin."J. Biol. Chem. 252:4942-4957(1977) [PubMed] [Europe PMC] [Abstract]
  9. "Mechanism of inhibition of activated protein C by protein C inhibitor."J. Biochem. 95:187-195(1984) [PubMed] [Europe PMC] [Abstract]
  10. "Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma."J. Biol. Chem. 261:13210-13215(1986) [PubMed] [Europe PMC] [Abstract]
  11. "Synthetic peptides bind to high-affinity thrombin receptors and modulate thrombin mitogenesis."Pept. Res. 1:65-73(1988) [PubMed] [Europe PMC] [Abstract]
  12. "Thrombophilic gene mutations and recurrent spontaneous abortion: prothrombin mutation increases the risk in the first trimester."Am. J. Reprod. Immunol. 46:124-131(2001) [PubMed] [Europe PMC] [Abstract]
  13. "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls."Arch. Neurol. 61:1652-1661(2004) [PubMed] [Europe PMC] [Abstract]
  14. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
  15. "rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce chemotaxis of human osteoblasts and microvascular endothelial cells."J. Orthop. Res. 23:680-685(2005) [PubMed] [Europe PMC] [Abstract]
  16. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
  17. "Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a placebo-controlled phase I/II study."Wound Repair Regen. 15:23-34(2007) [PubMed] [Europe PMC] [Abstract]
  18. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
  19. "A strategy for precise and large scale identification of core fucosylated glycoproteins."Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
  20. "Enrichment of glycopeptides for glycan structure and attachment site identification."Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
  21. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
  23. "The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment."EMBO J. 8:3467-3475(1989) [PubMed] [Europe PMC] [Abstract]
  24. "Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition."EMBO J. 9:2361-2365(1990) [PubMed] [Europe PMC] [Abstract]
  25. "The structure of a complex of recombinant hirudin and human alpha-thrombin."Science 249:277-280(1990) [PubMed] [Europe PMC] [Abstract]
  26. "Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms."Protein Sci. 2:1630-1642(1993) [PubMed] [Europe PMC] [Abstract]
  27. "Crystallographic structure of human gamma-thrombin."J. Biol. Chem. 269:22000-22006(1994) [PubMed] [Europe PMC] [Abstract]
  28. "The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin."EMBO J. 16:2977-2984(1997) [PubMed] [Europe PMC] [Abstract]
  29. "Unexpected crucial role of residue 225 in serine proteases."Proc. Natl. Acad. Sci. U.S.A. 96:1852-1857(1999) [PubMed] [Europe PMC] [Abstract]
  30. "Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate."J. Mol. Biol. 311:549-555(2001) [PubMed] [Europe PMC] [Abstract]
  31. "Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors."Org. Biomol. Chem. 4:2364-2375(2006) [PubMed] [Europe PMC] [Abstract]
  32. "Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin."J. Am. Chem. Soc. 129:10648-10649(2007) [PubMed] [Europe PMC] [Abstract]
  33. "Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles."Bioorg. Med. Chem. Lett. 18:2062-2066(2008) [PubMed] [Europe PMC] [Abstract]
  34. "Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex."Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008) [PubMed] [Europe PMC] [Abstract]
  35. "Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site."Br. J. Haematol. 54:245-254(1983) [PubMed] [Europe PMC] [Abstract]
  36. "Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273."J. Biol. Chem. 261:15045-15048(1986) [PubMed] [Europe PMC] [Abstract]
  37. "Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima."Biochemistry 26:1117-1122(1987) [PubMed] [Europe PMC] [Abstract]
  38. "Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin."Blood 69:565-569(1987) [PubMed] [Europe PMC] [Abstract]
  39. "Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382."Biochemistry 27:9160-9165(1988) [PubMed] [Europe PMC] [Abstract]
  40. "Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity."Biochemistry 28:2078-2082(1989) [PubMed] [Europe PMC] [Abstract]
  41. "Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity."Biochemistry 31:7457-7462(1992) [PubMed] [Europe PMC] [Abstract]
  42. "Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337-->Thr and Arg-388-->His)."Blood 80:2275-2280(1992) [PubMed] [Europe PMC] [Abstract]
  43. "Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia."Int. J. Hematol. 55:93-100(1992) [PubMed] [Europe PMC] [Abstract]
  44. "Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site."Blood Coagul. Fibrinolysis 5:841-844(1994) [PubMed] [Europe PMC] [Abstract]
  45. "Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala."Thromb. Haemost. 73:203-209(1995) [PubMed] [Europe PMC] [Abstract]
  46. "Characterization of single-nucleotide polymorphisms in coding regions of human genes."Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
  47. ErratumNat. Genet. 23:373-373(1999)
  48. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]