产品资料
  首页 >>> 产品目录 >>> 试剂 >>> Mybiosource

Coagulation factor V, Recombinant Protein

如果您对该产品感兴趣的话,可以
产品名称: Coagulation factor V, Recombinant Protein
产品型号:
产品展商: 其他品牌
产品文档: 无相关文档

简单介绍

Coagulation factor V, Recombinant Protein


Coagulation factor V, Recombinant Protein  的详细介绍
Product Name

Coagulation factor V (F5), Recombinant Protein

Popular Item
Full Product Name

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.
TOP
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
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
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.
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 13485:2003 and EN ISO 13485:2012 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.
TOP
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

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)
TOP
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]
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
TOP
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
TOP
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]
TOP
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
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.

Provides general information on the entry.


Research Articles on F5
1. This meta-analysis suggested that FVL was not a risk factor for sepsis and sepsis mortality
TOP
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
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.
TOP
TOP
产品留言
标题
联系人
联系电话
内容
验证码
点击换一张
注:1.可以使用快捷键Alt+S或Ctrl+Enter发送信息!
2.如有必要,请您留下您的详细联系方式!
相关产品
PDGF-AA, ELISA Kit
PDGF-AA, ELISA Kit
PDGF-AA, ELISA Kit
PDGF-AA, ELISA Kit
PDGF-AA, ELISA Kit
PDGF-AA, ELISA Kit
PDGF-AA, ELISA Kit
Microphthalmia Associated Transcription Factor (MITF), ELISA Kit
microphthalmia-associated transcription factor, Polyclonal Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, Blocking Peptide
CYP1B1, Polyclonal Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, Polyclonal Antibody
CYP1B1, cDNA Clone
CYP1B1, Antibody
Cytochrome P450 1B1, Antibody
Cytochrome P450 1B1, Polyclonal Antibody
Cytochrome P450 1B1, Polyclonal Antibody
Cytochrome P450 1B1, Antibody
Cytochrome P450 1B1, Antibody
Cytochrome P450 1B1 (CYP1B1), Polyclonal Antibody
Cytochrome P450 1B1 (CYP1B1), Polyclonal Antibody
Cytochrome P450 1B1 (CYP1B1), Polyclonal Antibody
Cytochrome P450 1B1 (CYP1B1), Polyclonal Antibody
Cytochrome P450 1B1 (CYP1B1), Polyclonal Antibody
Cytochrome P450 1B1 (CYP1B1), Polyclonal Antibody
Cytochrome P450 1B1 (CYP1B1), ELISA Kit
Cytochrome P450 1B1 (CYP1B1), ELISA Kit
Cytochrome P450 1B1 (CYP1B1), ELISA Kit
Cytochrome P450 1B1 (CYP1B1), ELISA Kit
Cytochrome P450 1B1 (CYP1B1), Antibody Pair Kit
Cytochrome P450 1B1 (CYP1B1), Active Protein
Cytochrome P450 1B1 (CYP1B1), Polyclonal Antibody
Cytochrome P450 1B1 (CYP1B1), RTU ELISA Kit
Cytochrome P450 1B1 (CYP1B1), Recombinant Protein
Optineurin, Polyclonal Antibody
AGPAT2, Polyclonal Antibody
AGPAT2, cDNA Clone
AGPAT2, cDNA Clone
AGPAT2, Polyclonal Antibody
AGPAT2, Polyclonal Antibody
AGPAT2, Blocking Peptide
AGPAT2, cDNA Clone

沪公网安备 31011202007343号