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Active Native Bovine Factor IX

Cat.No. : F9-266B
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Description : The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180). Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see figure) yields the intermediate IXa which is subsequently converted to the fully active form IXaβ by cleavage at site B. The NH2-terminal light chain (GLA and EGF domains) remains covalently attached to the COOH-terminal heavy chain by a disulfide bond. The serine protease catalytic triad (Ser-365, His 221, Asp-269) is located in the heavy chain. Factor IXaβ is the catalytic component of the "intrinsic factor Xase complex" (factor VIIIa/IXa/Ca2+/phospholipid) which proteolytically activates factor X to factor Xa.
Source : Plasma
Species : Bovine
Form : 50% (vol/vol) glycerol/H2O
Bio-activity : Clotting assay
Molecular Mass : 55400
Purity : >95% by SDS-PAGE. NOT tissue/cell culture grade. Not tested for endotoxin.
Characteristic : Extinction coefficient:12.0, Isoelectric point:3.7, Percent carbohydrate:0.26, Structure:single chain, NH2-terminal gla-domain, two EGF domains
Storage : -20°C
Tag : Non
Gene Name : F9 coagulation factor IX [ Bos taurus ]
Official Symbol : F9
Synonyms : coagulation factor I; Xchristmas factor; plasma thromboplastic component; coagulation factor IX (plasma thromboplastic component, Christmas disease, hemophilia B)
Gene ID : 280688
mRNA Refseq : NM_001103220
Protein Refseq : NP_001096690
Chromosome Location : Xq32-q33
Pathway : Complement and Coagulation Cascades, organism-specific biosystem; Complement and coagulation cascades, organism-specific biosystem; Extrinsic Pathway, organism-specific biosystem
Function : calcium ion binding; serine-type endopeptidase activity

Not For Human Consumption!

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Customer Reviews (3)

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Reviews
04/15/2021

    The short half-life makes this product very safe.

    10/10/2020

      This protein has a wide range of applications and can be used in a variety of experiments.

      03/27/2019

        The method of use is simple, which reduces the experimental time and improves the efficiency.

        Q&As (6)

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        What is the function of F9 protein? 12/18/2019

        The F9 protein is involved in step IX in the coagulation cascade, which works synergistically with other coagulation factors to promote the normal progress of blood clotting.

        How do genetic mutations in the F9 protein affect its function? 12/04/2019

        Mutations in the F9 gene may lead to loss of protein expression, structural abnormalities, or dysfunction, which in turn affect the normal function of the F9 protein.

        Do F9 protein mutations cause other diseases or affect other physiological processes? 05/27/2019

        F9 protein mutations are primarily associated with hemophilia B, but the specific mutation type and location may have different effects on an individual's clinical presentation.

        What diseases can F9 gene mutations cause? 05/22/2019

        Mutations in the F9 gene may cause hemophilia B, an inherited coagulation disorder in which patients lack the F9 protein or have low activity and are prone to abnormal bleeding.

        How is the activity of F9 protein determined? 04/08/2019

        The activity of the F9 protein is usually measured by coagulation time or by specific experimental methods (eg, prothrombin time, activated partial thromboplastin time, etc.).

        What is the structure of F9 protein? 01/31/2019

        F9 protein is a single-chain glycoprotein consisting of 415 amino acids. It contains a signaling peptide and multiple functional regions in which the Gla domain at the C-terminal binds to calcium ions and the EGF-like domain at the N-terminus participates in receptor binding and activation.

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