Native human Factor IX/PTC protein (ab81593)
Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Description
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Product name
Native human Factor IX/PTC protein
See all Factor IX/PTC proteins and peptides -
Biological activity
<1% Factor IXa activity. Assay is performed to determine percent contaminating IXa activity. IXa activity is based on a IXa standard curve. Chromagenic assay uses Spectrozyme-IXa (American Diagnostica) as substrate. Active site blocked by EGR. -
Purity
> 95 % SDS-PAGE. -
Expression system
Native -
Protein length
Full length protein -
Animal free
No -
Nature
Native -
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Species
Human -
Amino acids
47 to 461
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Specifications
Our Abpromise guarantee covers the use of ab81593 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
Functional Studies
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.40
Constituents: 0.476% HEPES, 0.87% Sodium chlorideThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- Christmas Disease
- Christmas factor
- Coagulant factor IX
see all -
Function
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. -
Tissue specificity
Synthesized primarily in the liver and secreted in plasma. -
Involvement in disease
Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:306900]; also known as Christmas disease.
Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide.
Defects in F9 are the cause of thrombophilia due to factor IX defect (THR-FIX) [MIM:300807]. A hemostatic disorder characterized by a tendency to thrombosis. -
Sequence similarities
Belongs to the peptidase S1 family.
Contains 2 EGF-like domains.
Contains 1 Gla (gamma-carboxy-glutamate) domain.
Contains 1 peptidase S1 domain. -
Domain
Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain. -
Post-translational
modificationsActivated by factor XIa, which excises the activation peptide.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. -
Cellular localization
Secreted. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (1)
ab81593 has been referenced in 1 publication.
- Fischer M et al. Novel in vitro inhibitory functions of potato tuber proteinaceous inhibitors. Mol Genet Genomics 290:387-98 (2015). PubMed: 25260821