Coagulation factor V Recombinant Protein | F5 recombinant protein

Recombinant Human Coagulation factor V

Cat. Num. AAA968507

• Gene Names: F5; FVL; PCCF; THPH2; RPRGL1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Coagulation factor V; Recombinant Human Coagulation factor V; Activated protein C cofactor; Proaccelerin; labile factor; F5 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1490-1614. Partial
• Sequence: MPSPSSPTLNDTFLSKEFNPLVIVGLSKDGTDYIEIIPKEEVQSSEDDYAEIDYVPYDDPYKTDVRTNINSSRDPDNIAAWYLRSNNGNRRNYYIAAEEISWDYSEFVQRETDIEDSDDIPEDTT
• Sequence Length: 1614

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for F5 recombinant protein

Central regulator of hostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.

Product Categories/Family for F5 recombinant protein

Cardiovascular

References

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Genet. 36:40-45(2004) Cloning of cDNAs coding for the heavy chain region and connecting region of human factor V, a blood coagulation factor with four types of internal repeats.Kane W.H., Ichinose A., Hagen F.S., Davie E.W.Biochemistry 26:6508-6514(1987) Human coagulation factor V, exon 13, missense mutation Asn713Ser.Kostka H.Studies on hereditary deficiency of coagulation factor V.Xie F., Cheng F., Zhu X.Zhonghua Xue Ye Xue Za Zhi 22:453-456(2001) Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin.Kane W.H., Davie E.W.Proc. Natl. Acad. Sci. U.S.A. 83:6800-6804(1986) The serine protease cofactor factor V is synthesized by lymphocytes.Shen N.L.L., Fan S.-T., Pyati J., Graff R., Lapolla R.J., Edgington T.S.J. Immunol. 150:2992-3001(1993) Mechanism of inhibition of activated protein C by protein C inhibitor.Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.J. 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Signal. 2:RA46-RA46(2009) Crystal structures of the membrane-binding C2 domain of human coagulation factor V.Macedo-Ribeiro S., Bode W., Huber R., Quinn-Allen M.A., Kim S.W., Ortel T.L., Bourenkov G.P., Bartunik H.D., Stubbs M.T., Kane W.H., Fuentes-Prior P.Nature 402:434-439(1999) A polymorphism in the human coagulation factor V gene.Bayston T.A., Ireland H., Olds R.J., Thein S.L., Lane D.A.Hum. Mol. Genet. 3:2085-2085(1994) Mutation in blood coagulation factor V associated with resistance to activated protein C.Bertina R.M., Koeleman B.P.C., Koster T., Rosendaal F.R., Dirven R.J., de Ronde H., van der Velden P.A., Reitsma P.H.Nature 369:64-67(1994) Detection of new polymorphic markers in the factor V gene association with factor V levels in plasma.Lunghi B., Iacoviello L., Gemmati D., Dilasio M.G., Castoldi E., Pinotti M., Castaman G., Redaelli R., Mariani G., Marchetti G., Bernardi F.Thromb. Haemost. 75:45-48(1996) Prevalence of the factor V Leiden mutation in hepatic and portal vein thrombosis.Mahmoud A.E.A., Elias E., Beauchamp N., Wilde J.T.Gut 40:798-800(1997) A novel mutation of Arg306 of factor V gene in Hong Kong Chinese.Chan W.P., Lee C.K., Kwong Y.L., Lam C.K., Liang R.Blood 91:1135-1139(1998) Factor V Cambridge a new mutation (Arg306-to-Thr) associated with resistance to activated protein C.Williamson D., Brown K., Luddington R., Baglin C., Baglin T.Blood 91:1140-1144(1998) Clinical significance of Arg306 mutations of factor V gene.Liang R., Lee C.K., Wat M.S., Kwong Y.L., Lam C.K., Liu H.W.Blood 92:2599-2600(1998) Characterization of single-nucleotide polymorphisms in coding regions of human genes.Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.Nat. Genet. 22:231-238(1999) ErratumCargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.Nat. Genet. 23:373-373(1999) Combinations of 4 mutations (FV R506Q, FV H1299R, FV Y1702C, PT 20210G/A) affecting the prothrombinase complex in a thrombophilic family.Castoldi E., Simioni P., Kalafatis M., Lunghi B., Tormene D., Girelli D., Girolami A., Bernardi F.Blood 96:1443-1448(2000) Five novel mutations in the gene for human blood coagulation factor V associated with type I factor V deficiency.van Wijk R., Nieuwenhuis K., van den Berg M., Huizinga E.G., van der Meijden B.B., Kraaijenhagen R.J., van Solinge W.W.Blood 98:358-367(2001) Novel factor V C2-domain mutation (R2074H) in two families with factor V deficiency and bleeding.Schrijver I., Houissa-Kastally R., Jones C.D., Garcia K.C., Zehnder J.L.Thromb. Haemost. 87:294-299(2002) Arg2074Cys missense mutation in the C2 domain of factor V causing moderately severe factor V deficiency molecular characterization by expression of the recombinant protein.Duga S., Montefusco M.C., Asselta R., Malcovati M., Peyvandi F., Santagostino E., Mannucci P.M., Tenchini M.L.Blood 101:173-177(2003) Factor V I359T a novel mutation associated with thrombosis and resistance to activated protein C.Mumford A.D., McVey J.H., Morse C.V., Gomez K., Steen M., Norstrom E.A., Tuddenham E.G.D., Dahlback B., Bolton-Maggs P.H.B.Br. J. Haematol. 123:496-501(2003) Meta-analysis of genetic studies in ischemic stroke thirty-two genes involving approximately 18,000 cases and 58,000 controls.Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.Arch. Neurol. 61:1652-1661(2004) Functional characterization of factor V-Ile359Thr a novel mutation associated with thrombosis.Steen M., Norstroem E.A., Tholander A.-L., Bolton-Maggs P.H.B., Mumford A., McVey J.H., Tuddenham E.G.D., Dahlbaeck B.Blood 103:3381-3387(2004) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 105990535
• NCBI GeneID: 2153
• NCBI Accession #: NP_000121.2
• NCBI GenBank Nucleotide #: NM_000130.4
• UniProt Accession #: P12259; Q14285; Q2EHR5; Q5R346; Q5R347; Q6UPU6; Q8WWQ6; A8K6E8
• Molecular Weight: 30.4 kDa
• NCBI Official Full Name: coagulation factor V preproprotein
• NCBI Official Synonym Full Names: coagulation factor V
• NCBI Official Symbol: F5
• NCBI Official Synonym Symbols: FVL; PCCF; THPH2; RPRGL1
• NCBI Protein Information: coagulation factor V
• UniProt Protein Name: Coagulation factor V
• Protein Family: Coagulation factor
• UniProt Gene Name: F5
• UniProt Entry Name: FA5_HUMAN

NCBI Description

This gene encodes an essential cofactor of the blood coagulation cascade. This factor circulates in plasma, and is converted to the active form by the release of the activation peptide by thrombin during coagulation. This generates a heavy chain and a light chain which are held together by calcium ions. The activated protein is a cofactor that participates with activated coagulation factor X to activate prothrombin to thrombin. Defects in this gene result in either an autosomal recessive hemorrhagic diathesis or an autosomal dominant form of thrombophilia, which is known as activated protein C resistance. [provided by RefSeq, Oct 2008]

Uniprot Description

factor V: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin. Defects in F5 are the cause of factor V deficiency (FA5D); also known as Owren parahemophilia. It is an hemorrhagic diastesis. Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2). THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis. Defects in F5 are a cause of susceptibility to Budd- Chiari syndrome (BDCHS). A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR); also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1). RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. Belongs to the multicopper oxidase family.

Protein type: Secreted; Protease; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 1q23

Cellular Component: endoplasmic reticulum lumen; ER to Golgi transport vesicle; ER-Golgi intermediate compartment membrane; extracellular region; extracellular space; Golgi membrane; membrane; plasma membrane

Molecular Function: copper ion binding; protein binding

Biological Process: blood circulation; blood coagulation; cellular protein metabolic process; COPII coating of Golgi vesicle; ER to Golgi vesicle-mediated transport; platelet activation; platelet degranulation; post-translational protein modification; protein amino acid N-linked glycosylation via asparagine

Disease: Budd-chiari Syndrome; Factor V Deficiency; Pregnancy Loss, Recurrent, Susceptibility To, 1; Stroke, Ischemic; Thrombophilia Due To Activated Protein C Resistance