protein

Recombinant Human Coagulation factor V

MBS968507

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Coagulation factor V

Coagulation factor V

Activated protein C cofactor; Proaccelerin, labile factor

coagulation factor V preproprotein; Coagulation factor V; coagulation factor V; coagulation factor V; Activated protein C cofactor; Proaccelerin, labile factor

F5

F5; F5; FVL; PCCF; THPH2; RPRGL1

FA5_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1490-1614

2224

MPSPSSPTLNDTFLSKEFNPLVIVGLSKDGTDYIEIIPK
EEVQSSEDDYAEIDYVPYDDPYKTDVRTNINSSRDPDNI
AAWYLRSNNGNRRNYYIAAEEISWDYSEFVQRETDIEDS
DDIPEDTT

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cardiovascular

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.

Complete cDNA and derived amino acid sequence of human factor V.Jenny R.J., Pittman D.D., Toole J.J., Kriz R.W., Aldape R.A., Hewick R.M., Kaufman R.J., Mann K.G.Proc. Natl. Acad. Sci. U.S.A. 84:4846-4850(1987) Structure of the gene for human coagulation factor V.Cripe L.D., Moore K.D., Kane W.H.Biochemistry 31:3777-3785(1992) SeattleSNPs variation discovery resourceThe DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. 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. Biochem. 95:187-195(1984) Coagulation Factor V contains copper ion.Mann K.G., Lawler C.M., Vehar G.A., Church W.R.J. Biol. Chem. 259:12949-12951(1984) Inactivation of human plasma kallikrein and factor XIa by protein C inhibitor.Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M., Bouma B.N.Biochemistry 27:4231-4237(1988) Posttranslational sulfation of factor V is required for efficient thrombin cleavage and activation and for full procoagulant activity.Pittman D.D., Tomkinson K.N., Michnick D., Selighsohn U., Kaufman R.J.Biochemistry 33:6952-6959(1994) Sulfation of tyrosine residues in coagulation factor V.Hortin G.L.Blood 76:946-952(1990) The mechanism of inactivation of human factor V and human factor Va by activated protein C.Kalafatis M., Rand M.D., Mann K.G.J. Biol. Chem. 269:31869-31880(1994) Characterization of semenogelin II and its molecular interaction with prostate-specific antigen and protein C inhibitor.Kise H., Nishioka J., Kawamura J., Suzuki K.Eur. J. Biochem. 238:88-96(1996) Protein C inhibitor secreted from activated platelets efficiently inhibits activated protein C on phosphatidylethanolamine of platelet membrane and microvesicles.Nishioka J., Ning M., Hayashi T., Suzuki K.J. Biol. Chem. 273:11281-11287(1998) Mutations in coagulation factors in women with unexplained late fetal loss.Martinelli I., Taioli E., Cetin I., Marinoni A., Gerosa S., Villa M.V., Bozzo M., Mannucci P.M.N. Engl. J. Med. 343:1015-1018(2000) Characterization of a novel human protein C inhibitor (PCI) gene transgenic mouse useful for studying the role of PCI in physiological and pathological conditions.Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H., Gabazza E.C., Ido M., Suzuki K.J. Thromb. Haemost. 2:949-961(2004) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Elucidation of N-glycosylation sites on human platelet proteins a glycoproteomic approach.Lewandrowski U., Moebius J., Walter U., Sickmann A.Mol. Cell. Proteomics 5:226-233(2006) Phosphoproteome of resting human platelets.Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.J. Proteome Res. 7:526-534(2008) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. 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.

105990535

NP_000121.2

NM_000130.4

P12259

30.41kD

Asparagine N-linked Glycosylation Pathway (1268714); Blood Clotting Cascade Pathway (198840); COPII (Coat Protein 2) Mediated Vesicle Transport Pathway (1268727); Cargo Concentration In The ER Pathway (1309087); Common Pathway Of Fibrin Clot Formation (1269371); Complement And Coagulation Cascades Pathway (198880); Complement And Coagulation Cascades Pathway (83073); Complement And Coagulation Cascades Pathway (484); ER To Golgi Anterograde Transport Pathway (1268726); Formation Of Fibrin Clot (Clotting Cascade) Pathway (1269368)

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]

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

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

860

0.05 mg (Mammalian-Cell)

1085