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Sigma Aldrich Fine Chemicals Biosciences Thrombin protease biotin t

Catalog No. 502905069
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Thrombin is an endolytic serine protease that selectively cleaves the Arg-Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.1 2The optimal cleavage sites for thrombin are as follows1. A-B-Pro-Arg--X-Y where A and B are hydrophobic amino acids and X and Y are nonacidic amino acids.2. Gly-Arg--GlyRecombinant human thrombin protease is expressed in human HEK 293 cells as a glycoprotein heterodimer. The DTT-reduced protein migrates as two bands of 31 kDa (heavy chain) and 6 kDa (light chain) on SDS-PAGE. This protein is manufactured in human cells with no serum. The human cells expression system allows human-like glycosylation and folding and often supports higher activity of the protein. This thrombin protease is useful for cleaving recombinant proteins that are expressed as fusion proteins with this sequence between the carrier domain and the protein of interest.

Catalog No. 50-290-5069 Supplier Sigma Aldrich Fine Chemicals Biosciences Supplier No. SAE01475KU
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Thrombin is an endolytic serine protease that selectively cleaves the Arg-Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.1 2The optimal cleavage sites for thrombin are as follows1. A-B-Pro-Arg--X-Y where A and B are hydrophobic amino acids and X and Y are nonacidic amino acids.2. Gly-Arg--GlyRecombinant human thrombin protease is expressed in human HEK 293 cells as a glycoprotein heterodimer. The DTT-reduced protein migrates as two bands of 31 kDa (heavy chain) and 6 kDa (light chain) on SDS-PAGE. This protein is manufactured in human cells with no serum. The human cells expression system allows human-like glycosylation and folding and often supports higher activity of the protein. This thrombin protease is useful for cleaving recombinant proteins that are expressed as fusion proteins with this sequence between the carrier domain and the protein of interest.

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