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Human Factor IXa Purified Active Site FITC Labeled

<strong>Human Factor IXa Purified Active Site FITC Labeled</strong>_x000D_ <strong>Catalog number:</strong> B2017439_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 100 µg_x000D_ <strong>Molecular Weight or Concentration:</strong> N/A_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> a molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -80¬∞C_x000D_ <strong>Keywords:</strong> N/A_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MŒ©-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Hamaguchi N, Charifson PS, Pedersen LG, Brayer GD, Smith KJ, Stafford DW. Expression and characterization of human factor IX. Factor IXthr-397 and factor IXval-397 J Biol Chem. 1991 Aug 15;266(23):15213-20._x000D_ 2: Bj√∂rk I, Jackson CM, J√∂rnvall H, Lavine KK, Nordling K, Salsgiver WJ. The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin J Biol Chem. 1982 Mar 10;257(5):2406-11._x000D_ 3: van der Graaf F, Greengard JS, Bouma BN, Kerbiriou DM, Griffin JH. Isolation and functional characterization of the active light chain of activated human blood coagulation factor XI J Biol Chem. 1983 Aug 25;258(16):9669-75._x000D_ 4: Larson PJ, Stanfield-Oakley SA, VanDusen WJ, Kasper CK, Smith KJ, Monroe DM, High KA. Structural integrity of the gamma-carboxyglutamic acid domain of human blood coagulation factor IXa Is required for its binding to cofactor VIIIa J Biol Chem. 1996 Feb 16;271(7):3869-76._x000D_ 5: Spitzer SG, Warn-Cramer BJ, Kasper CK, Bajaj SP. Replacement of isoleucine-397 by threonine in the clotting proteinase factor IXa (Los Angeles and Long Beach variants) affects macromolecular catalysis but not L-tosylarginine methyl ester hydrolysis. Lack of correlation between the ox brain prothrombin time and the mutation site in the variant proteins Biochem J. 1990 Jan 1;265(1):219-25._x000D_ 6: Tans G, Janssen-Claessen T, van Dieijen G, Hemker HC, Rosing J. Activation of factor IX by factor XIa--a spectrophotometric assay for factor IX in human plasma Thromb Haemost. 1982 Oct 29;48(2):127-32._x000D_ 7: Samis JA, Kam E, Nesheim ME, Giles AR. Neutrophil elastase cleavage of human factor IX generates an activated factor IX-like product devoid of coagulant function Blood. 1998 Aug 15;92(4):1287-96._x000D_ 8: Bezeaud A, Miyata T, Helley D, Zeng YZ, Kato H, Aillaud MF, Juhan-Vague I, Guillin MC. Functional consequences of the Ser334--&gt;Pro mutation in a human factor X variant (factor XMarseille) Eur J Biochem. 1995 Nov 15;234(1):140-7._x000D_ 9: Masys DR, Bajaj SP, Rapaport SI. Activation of human factor VII by activated factors IX and X Blood. 1982 Nov;60(5):1143-50._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/11071642">10: Neels JG, van Den Berg BM, Mertens K, ter Maat H, Pannekoek H, van Zonneveld AJ, Lenting PJ. Activation of factor IX zymogen results in exposure of a binding site for low-density lipoprotein receptor-related protein Blood. 2000 Nov 15;96(10):3459-65.</a>_x000D_ _x000D_ <strong>Products Related to Human Factor IXa Purified Active Site FITC Labeled can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>

Product Specifications

Short Description

Catalog Number: B2017439 (100 µg)

Weight

0.15

Length

2

Width

0.5

Height

0.5

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