PRSS7 Human

Protease Serine 7 Human Recombinant
Cat. No.
BT4611
Source
Escherichia Coli.
Synonyms
PRSS7,ENTK,Protease, Serine, 7 (Enterokinase), Transmembrane Protease, Serine 15, Serine Protease 7, Enteropeptidase, EC 3.4.21.9, Transmembrane Protease Serine 15,Enterokinase Catalytic Subunit, Proenterokinase, Enterokinase, EC 3.4.21.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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In Stock

Description

PRSS7 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 237 amino acids (785-1019 a.a.) and having a molecular mass of 26.4kDa. The PRSS7 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Protease Serine 7, alternatively referred to as PRSS7, plays a crucial role in initiating the activation of pancreatic proteolytic proenzymes, including trypsinogen, chymotrypsinogen, and procarboxypeptidase A. Specifically, PRSS7 catalyzes the conversion of trypsinogen into its active form, trypsin. Subsequently, trypsin triggers the activation of other proenzymes, such as chymotrypsinogen, procarboxypeptidases, and proelastases.
Description
Recombinant human PRSS7, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 237 amino acids (residues 785-1019). This protein has a molecular weight of 26.4 kDa. The purification of PRSS7 is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The PRSS7 protein solution is provided at a concentration of 1 mg/ml and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be stored at 4°C.
For extended storage, it is recommended to freeze the product at -20°C.
To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised.
Repeated freeze-thaw cycles should be avoided.
Purity
The purity of the protein is determined to be greater than 85% as assessed by SDS-PAGE analysis.
Synonyms
PRSS7,ENTK,Protease, Serine, 7 (Enterokinase), Transmembrane Protease, Serine 15, Serine Protease 7, Enteropeptidase, EC 3.4.21.9, Transmembrane Protease Serine 15,Enterokinase Catalytic Subunit, Proenterokinase, Enterokinase, EC 3.4.21.
Source
Escherichia Coli.
Amino Acid Sequence
MAIVGGSNAK EGAWPWVVGL YYGGRLLCGA SLVSSDWLVS AAHCVYGRNL EPSKWTAILG LHMKSNLTSP QTVPRLIDEI VINPHYNRRR KDNDIAMMHL EFKVNYTDYI QPICLPEENQ VFPPGRNCSI AGWGTVVYQG TTANILQEAD VPLLSNERCQ QQMPEYNITE NMICAGYEEG GIDSCQGDSG GPLMCQENNR WFLAGVTSFG YKCALPNRPG VYARVSRFTE WIQSFLH

Product Science Overview

Structure and Function

PRSS7 catalyzes the conversion of trypsinogen to trypsin. Trypsin, in turn, activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases . This cascade of enzyme activation is essential for the digestion of proteins in the small intestine. The precise regulation of these enzymes is critical for maintaining digestive health and preventing conditions such as pancreatitis.

Recombinant Production

The recombinant production of proteases, including PRSS7, has become a significant focus due to the increasing demand for these enzymes in various industries. Recombinant proteases are produced using microbial systems, which offer advantages such as high-level expression and compatibility with downstream applications . The production process involves the insertion of the gene encoding PRSS7 into a suitable host organism, such as Escherichia coli or Bacillus species, which then expresses the enzyme.

Applications

Recombinant PRSS7 has several applications in biotechnology and medicine. In the medical field, it is used in research related to digestive enzymes and their role in various diseases. In biotechnology, PRSS7 is utilized in the production of other enzymes and in processes that require precise proteolytic activity.

Advances in Research

Recent advancements in protease engineering, including rational design and directed evolution, have improved the efficiency and stability of recombinant proteases . These techniques allow for the modification of PRSS7 to enhance its properties, making it more suitable for industrial and medical applications.

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