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ProteoSure™ Modified Trypsin, Autolysis-Resistant, Sequencing Grade, 2x 100 μg, 14-SRT-200UG, Marvelgent biosciences (CAT#: STEM-GT-3041-LGZ)

Highlights

Recombinant pure enzyme, no chymotrypsin nor the need of TPCK treatment
Autolysis-resistant

Cat Number: STEM-GT-3041-LGZ

Application: It is suitable for in-solution or in-gel protein digestion in applications:<br /><br />Peptide sequencing and tryptic mapping<br />Protein identification by peptide mass fingerprinting or MS/MS spectral matching.<br />Protein-structure studies

Model: 14-SRT-200UG

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Description

ProteoSure™ Sequencing Grade Trypsin is a highly purified variant of porcine tryptophan that has been genetically improved and chemically modified for highest self-resistance and maximum specificity for protein research applications.

ProteoSure™ recombinant porcine trypsin variants were expressed and purified from E. coli in a tightly controlled system. Enzymes are not affected by contamination, such as chymoprotease. Therefore, it does not require treatment with L-(tosylamia-2-2-2-phenyl)ethylchloromethylketone (TPCK), unlike other sequencing-grade trypsin proteases derived from animal pancreas extracts and Treated (TPCK) to remove chymoprotease activity.

The trypsin variant of ProteoSure™ Recombinant Porphyrin is genetically engineered and further modified by reduction to achieve greater resistance to lytic digestion, compared to other modified native trypsin proteases.

Trypsin is a serine that specifically hydrolyzes peptide bonds in the carboxyl groups of lysine and arginine residues. Native trypsin, known as "protease", is also affected by autolytic digestion. Autolunk results in an enzyme form, such as enzyme stability and efficiency. This form of the enzyme can be further autodegraded to produce pseudosine (also known as "acid-trypsin)", which exhibits an expanded specificity, including a chymoprotease-like activity. The stability, selectivity, and activity of this enzyme are critical for regenerative protein digestion and mass spectroscopic protein recognition.

Trypsin can be combined with Lysyl Endopeptidase (Lys-C), which has been shown to improve sequence coverage for peptide mapping.

Specification

Size: 2x 100 μg
CAS #: 9002-07-07
Enzyme Commission #: 3.4.21.4
Molecular weight: 23.8 kDa
Origin of species: Porcine
Source: E.coli
Optimum pH: 7.8-8.7
Purified by: HPLC
Physical form: 0.5 mg/mL solution in 50mM HAc. May appear as fluffy solid.
Specific activity: ≥4500 USP /mg protein, autolytic activity minimized by reductive methylation.
Unit definition: One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0 mL at pH7.6 and 25℃, with BAEE as a substrate (1 cm light path).
Purity: ≥99% by HPLC
Contaminant activity: No chymotrypsin, carboxypeptidase A, or other protease contaminants.
Storage: The solution should be stored at -70°C, It is stable within 24 months. Greater than 95% enzymatic activity retains after 5 repeated freezing-and-thawing cycles.
Intended use: For research only. Not intended for any human or animal diagnostic or therapeutic use.

Features

Recombinant pure enzyme, no chymotrypsin nor the need of TPCK treatment
Autolysis-resistant

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