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F5 recombinant protein :: Coagulation factor V Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS968507
SDS-PAGE
Unit / Price
0.01 mg (E-Coli)  /  $110 +1 FREE 8GB USB
0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

Coagulation factor V (F5), Recombinant Protein

★Popular Item★
 Also Known As   

Recombinant Human Coagulation factor V

 Product Synonym Names    Activated protein C cofactor; Proaccelerin, labile factor
 Product Gene Name   

F5 recombinant protein

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 Sequence Positions    1490-1614aa; Partial
 Sequence    MPSPSSPTLN DTFLSKEFNP LVIVGLSKDG TDYIEIIPKE EVQSSEDDYA EIDYVPYDDP YKTDVRTNIN SSRDPDNIAA WYLRSNNGNR RNYYIAAEEI SWDYSEFVQR ETDIEDSDDI PEDTT
 OMIM    188055
 3D Structure    ModBase 3D Structure for P12259
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 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
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 Purity/Purification    Greater than 90% as determined by SDS-PAGE. (lot specific)
 Form/Format    Liquid containing glycerol
 Tag Information    This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
 Sterility    Sterile filter available upon request.
 Endotoxin    Low endotoxin available upon request.
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 Preparation and Storage    Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of F5 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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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
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 SDS-PAGE of F5 recombinant protein    F5 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for F5. It may not necessarily be applicable to this product.
 NCBI GI #    105990535
 NCBI GeneID    2153
 NCBI Accession #    NP_000121.2 [Other Products]
 NCBI GenBank Nucleotide #    NM_000130.4 [Other Products]
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 UniProt Primary Accession #    P12259 [Other Products]
 UniProt Secondary Accession #    Q14285; Q2EHR5; Q5R346; Q5R347; Q6UPU6; Q8WWQ6; A8K6E8 [Other Products]
 UniProt Related Accession #    P12259 [Other Products]
 Molecular Weight    30.41kD
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 NCBI Official Full Name    coagulation factor V preproprotein
 NCBI Official Synonym Full Names    coagulation factor V
 NCBI Official Symbol    F5 [Similar Products]
 NCBI Official Synonym Symbols   
FVL; PCCF; THPH2; RPRGL1
[Similar Products]
 NCBI Protein Information    coagulation factor V
 UniProt Protein Name    Coagulation factor V
 UniProt Synonym Protein Names   
Activated protein C cofactor; Proaccelerin, labile factor
 Protein Family    Coagulation factor
 UniProt Gene Name    F5 [Similar Products]
 UniProt Entry Name    FA5_HUMAN
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 NCBI Summary for F5    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]
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 UniProt Comments for F5    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
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Product References and Citations for F5 recombinant protein

   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.
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 Research Articles on F5    1. This meta-analysis suggested that FVL was not a risk factor for sepsis and sepsis mortality
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 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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Products associated with F5 recombinant proteinPathways associated with F5 recombinant protein
 Reference Product  PubMed Publications
 F10 recombinant protein  >42 publications with F5 and F10
 PROC recombinant protein  >23 publications with F5 and PROC
 SERPINE1 recombinant protein  >12 publications with F5 and SERPINE1
 SERPINC1 recombinant protein  >9 publications with F5 and SERPINC1
 VWF recombinant protein  >8 publications with F5 and VWF
 PROS1 recombinant protein  >4 publications with F5 and PROS1
 PLG recombinant protein  >1 publications with F5 and PLG
 Products by Pathway  Pathway Diagram
 Asparagine N-linked Glycosylation Pathway antibodies  Asparagine N-linked Glycosylation Pathway Diagram
 Blood Clotting Cascade Pathway antibodies  Blood Clotting Cascade Pathway Diagram
 COPII (Coat Protein 2) Mediated Vesicle Transport Pathway antibodies  COPII (Coat Protein 2) Mediated Vesicle Transport Pathway Diagram
 Cargo Concentration In The ER Pathway antibodies  Cargo Concentration In The ER Pathway Diagram
 Common Pathway Of Fibrin Clot Formation antibodies  Common Pathway Of Fibrin Clot Formation Diagram
 Complement And Coagulation Cascades Pathway antibodies  Complement And Coagulation Cascades Pathway Diagram
 Complement And Coagulation Cascades Pathway antibodies  Complement And Coagulation Cascades Pathway Diagram
 Complement And Coagulation Cascades Pathway antibodies  Complement And Coagulation Cascades Pathway Diagram
 ER To Golgi Anterograde Transport Pathway antibodies  ER To Golgi Anterograde Transport Pathway Diagram
 Formation Of Fibrin Clot (Clotting Cascade) Pathway antibodies  Formation Of Fibrin Clot (Clotting Cascade) Pathway Diagram
Diseases associated with F5 recombinant proteinOrgans/Tissues associated with F5 recombinant protein
 Disease Name  Pubmed Publications
 Cardiovascular Diseases Antibodies  >113 publications with F5 and Cardiovascular Diseases
 Thrombosis Antibodies  >70 publications with F5 and Thrombosis
 Immune System Diseases Antibodies  >51 publications with F5 and Immune System Diseases
 Blood Coagulation Disorders Antibodies  >40 publications with F5 and Blood Coagulation Disorders
 Venous Thrombosis Antibodies  >33 publications with F5 and Venous Thrombosis
 Inflammation Antibodies  >33 publications with F5 and Inflammation
 Thromboembolism Antibodies  >31 publications with F5 and Thromboembolism
 Venous Thromboembolism Antibodies  >28 publications with F5 and Venous Thromboembolism
 Liver Diseases Antibodies  >25 publications with F5 and Liver Diseases
 Factor V Deficiency Antibodies  >23 publications with F5 and Factor V Deficiency
 Organ/Tissue Name  Pubmed Publications
 Blood Antibodies  >384 publications with F5 and Blood
 Brain Antibodies  >212 publications with F5 and Brain
 Liver Antibodies  >65 publications with F5 and Liver
 Thymus Antibodies  >43 publications with F5 and Thymus
 Heart Antibodies  >41 publications with F5 and Heart
 Intestine Antibodies  >37 publications with F5 and Intestine
 Lung Antibodies  >37 publications with F5 and Lung
 Kidney Antibodies  >34 publications with F5 and Kidney
 Eye Antibodies  >31 publications with F5 and Eye
 Embryonic Tissue Antibodies  >22 publications with F5 and Embryonic Tissue
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