Analytical Data
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Gene name
Cationic trypsin
- Application
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Alternative Names
Cationic trypsin; EC 3.4.21.4
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Species
Dog
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Source
E. coli
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Tag
N-His;N-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P06871
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Expression Region
I24-N246
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AA Sequence
IVGGYTCSRNSVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSRIQVRLGEYNIAVSEGGEQFINAAKIIRHPRYNANTIDNDIMLIKLSSPATLNSRVSAIALPKSCPAAGTQCLISGWGNTQSIGQNYPDVLQCLKAPILSDSVCRNAYPGQISSNMMCLGYMEGGKDSCQGDSGGPVVCNGELQGVVSWGAGCAQKGKPGVSPKVCKYVSWIQQTIAAN
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Protein Length
Full Length of Mature Protein
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Cationic trypsin, a serine protease primarily found in the pancreas, plays a crucial role in digestion by cleaving peptide bonds in proteins, thus facilitating nutrient absorption. Its enzymatic activity is characterized by a preference for basic amino acids, making it essential for the proper functioning of the gastrointestinal system. The study of cationic trypsin is significant not only for understanding digestive processes but also for its potential applications in biotechnology and medicine. Recombinant protein technology has enabled the production of cationic trypsin in various expression systems, which allows researchers to study its structure, function, and interactions in greater detail. This has implications in therapeutic developments, particularly in conditions related to digestive disorders or pancreatic dysfunctions. Furthermore, the biochemical properties of trypsin make it a useful tool in various industrial processes, including protein purification and enzyme assays. Thus, investigating the recombinant form of cationic trypsin can lead to advancements in both basic science and applied research, offering insights into enzyme regulation and contributing to the development of novel therapeutic strategies.
