|Calculated MW||37 kDa|
|Other Names||Activated Factor IIa|
|Results||>3000 units/mg protein.|
|Application Notes||A working stock solution can be prepared by adding 1 mL buffered saline, pH 7.4 (ex. 25 mM HEPES, 150 mM NaCl, 0.1% PEG 8000, pH 7.4). Further dilution should be made in buffer containing a suitable stabilizing agent such as 0.1%-1% Prionex, BSA, or PEG.|
|Storage||-20°C; Lyophilized from a buffer composed of 20 mM Bis-Tris, 150 mM NaCl and 0.1% PEG 8000, pH 6.5.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
firstname.lastname@example.org, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 188.8.131.52) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
Degen S.J.F.,et al.Biochemistry 26:6165-6177(1987).
Wang W.,et al.Haemophilia 10:94-97(2004).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Suzuki Y.,et al.Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
Degen S.J.F.,et al.Biochemistry 22:2087-2097(1983).
If you have used an Abgent product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at email@example.com.