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Restriction enzymes, modifying enzymes, buffering solutions, inhibitors, and substrates for use in clinical, research, and general laboratory procedures.
Heparinase is an inducible non-extracellular heparin-degrading enzyme. Three types of heparinises are produced by flavobacterium heparinum and contains specific sequences of heparin.
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Recombinant human pre-activated Matrix Metalloproteinase-9 (MMP-9) is expressed in human HEK 293 cells as a glycoprotein. The DTT-reduced protein migrates as a ~67 kDa polypeptide 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 specific activity of the protein. The protein is produced with no artificial tags.
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Heparinase is an inducible non-extracellular heparin-degrading enzyme. Three types of heparinises are produced by flavobacterium heparinum and contains specific sequences of heparin.
Encompass Procurement Services Non-distribution item offered as a customer accommodation; additional freight charges may apply. Learn More
D-Luciferin is mainly produced in bioluminescent organisms. It can simply circulate across the blood testis barrier blood brain barrier and the blood placenta barrier. This small molecule is sensitive to light and oxygen. D-Luciferin is also sensitive to moisture in its powder form.
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A cofactor in the electron transport chain; decreased levels due to genetic mutations in its synthesis enzymes lead to encephalopathy, cerebellar ataxia, infantile multisystemic form, nephropathy, and isolated myopathy
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The BirA biotin-protein ligase adds d-biotin covalently to biotin-acceptor peptides/proteins via an ATP intermediate (biotinyl 5'-adenylate) in a highly efficient and targeted manner. This kit includes 300 ug of BirA enzyme for those who require larger scale reactions or more frequent use of the BirA biotinylation reaction in their work.
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Small and Specialty Supplier Partner Small and/or specialty supplier based on Federal laws and SBA requirements. Learn More
A synthetic peptide that that selectively, reversibly, and substrate-competitively inhibits PKCζ activity and, thus, is used to delineate the signaling functions of PKCζ
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Endoglycosidase H is a recombinant glycosidase which cleaves within the chitobiose core of high mannose and some hybrid oligosaccharides from N-linked glycoproteins. It is a recombinant glycosidase cloned from Streptomyces plicatus and overexpressed in E. coli.
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Endoglycosidase H is a recombinant glycosidase which cleaves within the chitobiose core of high mannose and some hybrid oligosaccharides from N-linked glycoproteins. It is a recombinant glycosidase cloned from Streptomyces plicatus and overexpressed in E. coli.
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EndoS is an endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes N-linked glycans in the Fc-region of native IgG. It specifically deglycosylates the conserved N-glycans on the Fc region of IgG by hydrolyzing the chitobiose core (at the beta -1,4 linkage between the two N-acetylglucosamines) of the N-glycans, cleavage leave one GlcNAc residue remaining attached to the asparagine residue on the peptide backbone.
Encompass Procurement Services Non-distribution item offered as a customer accommodation; additional freight charges may apply. Learn More