Analytical Data
-
Gene name
F12
- Application
-
Alternative Names
F12；CFBP；FAM125A；Multivesicular body subunit 12A
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P00748
-
Expression Region
20-372aa
-
AA Sequence
IPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTR
-
Molecular Weight
43.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
F12 (Factor XII) is a crucial protein involved in the intrinsic pathway of coagulation, playing a vital role in the initiation of blood clotting. Research into F12 has gained significant attention due to its implications in various pathological conditions, including thrombosis, sepsis, and inflammation. Unlike other coagulation factors, F12 is unique in that it can activate without the need for prior tissue injury, leading to the potential for inappropriate activation and thrombosis in certain individuals. The understanding of F12's structure and function has evolved, with studies exploring its role in the cascade of coagulation and the fibrinolytic system. Recent advancements in recombinant technology have enabled the development of F12-related therapeutic proteins, aiming to modulate its activity in clinical settings. The research on F12 is critical, not only for understanding coagulation disorders but also for developing innovative therapeutic strategies to prevent and treat thrombotic diseases, making it a promising target in hematology and cardiovascular medicine.
