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Mass Spectrometry & Sequencing

Download the Sample Preparation for Mass Spectrometry Handbook for full list of  lysates & blots

We offer a variety of reagents for mass spectrometry and sequencing including mass spectrometry grade Trypsin and highly purified preparations of other proteases, including SG-Lysine-C.

 
Our InGel is a highly reliable method for the proteolytic digestion of proteins in gel for subsequent analysis by mass spectrometry. InGelArray is also available for high throughput in gel digestion of protein spots for mass spectrometry. FOCUSFASTsilver produces crystal clear backgrounds and maximal peptide recovery needed for critical analysis by mass spectrometry.

 

A large selection of mass spectrometry and sequencing accessories are also available. Our Proteomic Grade Water removes contamination worries and improves reliability of 2D gel analysis. Trypsin Digestion Mix provides optimal buffered conditions for in gel trypsin digestion. Proteomic grade microfuge tubes can also be found among our accessories.

SG-Chymotrypsin™ is a serine endopeptidase, which predominantly cleaves peptide bonds on the carboxy side of tyrosine, phenylalanine and tryptophan. In addition, chymotrypsin has a low catalytic activity against the carboxy side of leucine, methionine, alanine, aspartic and glutamic acids. It ..
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SG-Glutamic-C™ is a serine endopeptidase, from S. aureus V8, that is highly specific for the cleavage of peptide bonds at the carboxy side of either aspartic or glutamic acid, depending on the buffer used. In Tris-HCl buffer, in particular in the absence of phosphate ions, the enzyme is specif..
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SG-Lysine-C™ endopeptidase, from Lysobacter enzymogenes, is a serine protease highly specific in cleaving peptide bonds at the carboxy side of lysine. Highly purified preparations of SG-Lysine-C™ are chemically modified making the enzyme resistant to autolysis and stabilizing its enzymat..
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Trypsin is a serine protease that cleaves peptides on C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7.0-8.0. Trypsin is inhibited by serine protease inhibitors including TLCK (N-p-tosyl-L-lysine chloromethyl ketone), PMSF (phenylmethanesulfonyl fluoride),..
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Model:
A Chemically Modified, TPCK treated, Affinity Purified Trypsin. G-Biosciences' Mass Spectrometry Grade Trypsin is chemically methylated to yield an enzymatically active protein with maximum trypsin specificity and extreme resistance to autolysis. In addition, the modified trypsin is TPCK tr..
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