Coagulation Factor IX (human, recombinant)

Coagulation Factor IX is a vitamin K-dependent plasma serine protease involved in the intrinsic and extrinsic pathways of the blood coagulation cascade. It is composed of an N-terminal domain containing carboxylated glutamic acid residues (Gla domain), two EGF-like domains, a linker module, and a C-terminal trypsin-like catalytic peptidase domain. Coagulation Factor IX is produced as an inactive precursor, which is activated to Factor IXabeta following signal peptide cleavage, glycosylation, and further cleavage by Factor XIa or VIIa. In its activated form, Factor IXabeta, in complex with Factor VIIIa, converts Factor X to Factor Xa, the activated form. Mutations in F9, the gene encoding Factor IX, are responsible for the X-linked bleeding disorder hemophilia B, characterized by mild to severe deficits in blood coagulation. Cayman's Coagulation Factor IX (human, recombinant) protein can be used for enzyme activity applications. This protein consists of 444 amino acids, has a calculated molecular weight of 50 kDa, and a predicted N-terminus of Thr29 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 60-80 kDa due to glycosylation.Synonyms: Christmas Factor, Coagulation Factor 9, Factor IX, FIX, Plasma Thromboplastin Component, PTC. Purity: >95% as determined by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg, determined by the LAL endotoxin assay. Source: Active recombinant human C-terminal His-tagged coagulation factor IX expressed in HEK293 cells. Amino Acids: 29-461. MW: 50 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4. Specific Activity: >20 pmols/min/µg. UniProt Accession #: P00740.