Recombinant Human Trypsin-1 Protein

Name: Recombinant Human Trypsin-1 Protein
Brand: Beta LifeScience
SKU: BL-4842PS
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag	N/A
Host Species	Human
Synonym	Protease Serine 1 (Trypsin 1), TRY1, Cationic Trypsinogen, TRP1, TRYP1, TRY4, beta-trypsin, Digestive Zymogen, Nonfunctional Trypsin 1, Trypsinogen 1, Trypsinogen A, EC 3.4.21.4.
Background	Trypsin-1, which belongs to the trypsin family of serine proteases, is localized to the T cell receptor beta locus on chromosome 7. Trypsin-1 is secreted by the pancreas and cleaved to its active form in the small intestine. Trypsin-1 operates on peptide linkages involving the carboxyl group of lysine or arginine. Alterations are the cause for hereditary pancreatitis.
Description	Trypsin-1 Human Recombinant expressed in CHO cells is a 24.1kDa single polypeptide chain consisting of 224a.a..
Source	CHO
AA Sequence	IVGGYNCEEN SVPYQVSLNS GYHFCGGSLI NEQWVVSAGH CYKSRIQVRL GEHNIEVLEG NEQFINAAKI IRHPQYDRKT LNNDIMLIKL SSRAVINARV STISLPTAPP ATGTKCLISG WGNTASSGAD YPDELQCLDA PVLSQAKCEA SYPGKITSNM FCVGFLEGGK DSCQGDSGGP VVCNGQLQGV VSWGDGCAQK NKPGVYTKVY NYVKWIKNTI AANS.
Purity	>95% as determined by SDS-PAGE.
Endotoxin	<1.0 EU per μg by the LAL method.
Bioactivity	1 unit hydrolyzes 1 µmole of Na-Benzoyl-D,L-arginine 4-nitroanilide (BANI) per minute at 37°C, pH 8.0, in the presence of 10mM calcium.The specific activity is >1,000 Units per mg protein as measured under the described conditions.
Formulation	The Trypsin-1 filtered 0.22um solution contains 20mM TRIS-HCl buffer pH 7.2.
Stability	Recombinant protein is stable for 12 months at -70°C
Usage	For Research Use Only
Storage	Store at 4°C if entire vial will be used within 2-4 weeks.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.