Thrombin, Alpha, FPRCK, Bovine Active Protein

Proteolytic Activation of Prothrombin: The serine protease a-thrombin is produced by proteolytic activation of the zymogen, prothrombin. The enzyme complex, prothrombinase, catalyzes the proteolysis of two peptide bonds in prothrombin, which gives rise to an NH2-terminal derived F1.2 region and the heterodimer, a-thrombin.

Thrombin is a two chain enzyme composed of an NH2-terminal "A" chain (Mr 6000) and a COOH-terminal "B" chain (Mr 31,000) which remain covalently associated through a single disulfide bond. Human thrombin is 13 amino acids shorter than the bovine thrombin due to a thrombin cleavage site on the human protein that is not present in the bovine protein.
Thrombin is also utilized for site specific cleavage of fusion proteins expressed in bacteria (9-11). A thrombin sensitive site is incorporated between the recombinant protein of interest and peptides or proteins which facilitate purification and/or expression. The target protein is released from the expressed hybrid by cleavage with thrombin. Thrombin can then be easily removed by affinity chromatography.

Small volumes of Thrombin, alpha, FPRCK, Bovine active protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS635143 is an active protein targeting Thrombin, alpha, FPRCK, Bovine. Host: Bovine plasma.