Recombinant Human Coagulation Factor IX (Catalog # 9260-SE)is measured by its ability to cleave the fluorogenic peptide substrate,MCA-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002).
Recombinant Human Coagulation Factor IX Protein, CF Summary
Details of Functionality
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH<SUB>2</SUB> (Catalog # <a class=NoLineLink href='http://www.rndsystems.com/product_results.aspx?k=ES002'>ES002</a>).<br />The specific activity is >30 pmol/min/μg, as measured under the described conditions.<br /><br />
<1.000 EU per 1 µg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Enzyme Activity
Theoretical MW
75 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
86-104 kDa, reducing conditions
Publications
Read Publication using 9260-SE in the following applications:
Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Buffer
Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Coagulation Factor IX Protein, CF
Christmas Factor
Coagulation Factor IX
EC 3.4.21
EC 3.4.21.22
F9
factor 9
FIX
HEMB
MGC129641
MGC129642
P19
Plasma Thromboplastic Component
Plasma thromboplastin component
PTC
THPH8
Background
Coagulation Factor IX, also known as Christmas Factor, is a secreted by the liver and plays a key role in the activation of the intrinsic clotting cascade (1). Factor IX consists of a Gla domain, two tandem EGF-like domains, an activation peptide, and an S1 serine protease domain (2). Mature human Factor IX shares approximately 81% amino acid sequence identity with mouse and rat Factor IX. Alternative splicing generates an additional isoform that lacks the first EGF-like domain. The Gla domain is modified by Vitamin K-dependent gamma-carboxylation and mediates the association of Factor IX with phospholipid bilayers (3, 4). The activation peptide is removed by Factor XIa mediated cleavage, resulting in heavy and light chains that remain disulfide-linked (5). Factor IX can also be activated by proteolytic factors in multiple snake venoms (6, 7). Active Factor IX associates with Factor VIIIa on the platelet surface where it cleaves and activates Factor X, leading to Fibrin deposition and clot formation (8-10). The human Factor IX gene is highly polymorphic, and Hemophilia B can be caused by X-linked deficiency of Factor IX activity (11-14).
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