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詳細
Anti-Factor VII antibody, mouse monoclonal (mouse) IgG1 isotype) is derived from the HVII-1 hybridoma produced by the fusion of mouse Sp2/0-Ag14 myeloma cells and splenocytes from immunized BAB/c mice. Human coagulation factor VII contains 10 gamma-carboxyglutamic acid residues (Gla), located at the N-terminal region of the molecule. The activated factor VII (factor VIIa) also consists of a light chain with the Gla-domain and an epidermal growth factor domain, which is linked by a disulfide bond to a heavy chain, containing the serine protease catalytic domain.
特異性
抗体は、二価カチオンの存在または非存在下で第VII因子の軽鎖上のエピト-プを認識します。クロ-ンHVII-1(MC1476/E.A.8.1とも表される)は、第VII因子の精製や第VII因子を枯渇させたヒト血漿の調製に利用されます。
免疫原
正常ヒト血漿プ-ル由来第VII因子。
アプリケーション
Anti-Factor VII antibody, Mouse monoclonal has been used in:
- the preparation of factor VII - depleted plasma and for purification
- sandwich-type immunoassays
- the evaluation of patients with hereditary factor VII deficiency by an enzyme linked immunosorbent assay (ELISA) or radio immunosorbent assay (RIA)
- the assay of factor VII level in patients with liver disease (a sensitive parameter of liver dysfunction)
- epidemiological studies of the importance of factor VII level as a risk factor for coronary heart disease, cerebrovascular disease and peripheral vascular diseases
- the determination of the activity state of factor VII in in vivo samples when used with a clotting assay
- flow cytometry
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Flow cytometry/Cell sorting (1 paper)
Flow cytometry/Cell sorting (1 paper)
Monoclonal Anti-Factor VII antibody is suitable for flow cytometry analysis to study the behavior of TF-fVIIa secreted by ovarian cancer cells was associated with microparticles (MPs). It is also suitable for western blot at a dilution of 1:4,000 and indirect ELISA.
生物化学的/生理学的作用
Factor VII is a single-chain vitamin K-dependent glycoprotein in human coagulation. It has a molecular weight of ∼50,000Da, present in plasma in trace quantities. It is predominantly synthesized in liver and depends on the posttranslational γ−carboxylation of specific glutamic residues located near the NH2-terminus of the molecule. It is a serine protease zymogen and for activation it requires proteolytic cleavage in the disulfide-linked, two-chain form, Factor VIIa, by Factor Xa, Factor IXa, thrombin and Factor XIIa or β XIIa.
物理的形状
10 mM HEPESバッファ-溶液(pH 7.4, 140 mM 塩化ナトリウム, 0.05%アジ化ナトリウム含有)。
免責事項
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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保管分類コード
10 - Combustible liquids
WGK
nwg
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
F8146-.5ML:
F8146-BULK:
F8146-VAR:
F8146-.2ML:
The Journal of biological chemistry, 255(4), 1242-1247 (1980-02-25)
Blood coagulation Factor VII was purified 100,000-fold from fresh frozen human plasma to apparent homogeneity with a yield of 30% based on coagulation assay. The molecular weight estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was 48,000. Factor VII is composed
Regulated readthrough: A new method for the alternative tagging and targeting of recombinant proteins
Journal of Biotechnology, 125(4), 516-528 (2006)
Journal of biotechnology, 125(4), 516-528 (2006-05-10)
We report here a new method for the alternative peptide tagging of recombinant proteins from mammalian cell lines. This method, which we called regulated readthrough, exploits the property of aminoglycoside antibiotics to promote translational readthrough of nonsense codons. The basic
Structural biology of factor VIIa/tissue factor initiated coagulation
Frontiers in Bioscience, 17, 2476-2476 (2012)
Blood, 89(3), 767-775 (1997-02-01)
We report the development of an enzyme-linked immunosorbent assay (ELISA) that is specific for factor VIIa (FVIIa). This assay uses a neoantigen specific capture antibody directed to the amino acid peptide sequence N terminal to the FVII cleavage activation site.
ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.
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