Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
Product nameNative Human Factor IXa protein (FITC)
See all Factor IXa proteins and peptides
Purity> 95 % SDS-PAGE.
ab92599 is > 98% pure by SDS-PAGE.
Protein lengthFull length protein
ConjugationFITC. Ex: 493nm, Em: 528nm
Our Abpromise guarantee covers the use of ab92599 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesProtect from light.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 2.38% HEPES, 0.0292% EDTA, 0.58% Sodium chloride
- Christmas factor
- Coagulant factor IX
- Coagulation factor IX
FunctionFactor 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 specificitySynthesized primarily in the liver and secreted in plasma.
Involvement in diseaseDefects 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 similaritiesBelongs to the peptidase S1 family.
Contains 2 EGF-like domains.
Contains 1 Gla (gamma-carboxy-glutamate) domain.
Contains 1 peptidase S1 domain.
DomainCalcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.
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.
- Information by UniProt
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.
ab92599 has not yet been referenced specifically in any publications.