PGPEP1 Human

Pyroglutamyl-Peptidase I Human Recombinant
Cat. No.
BT24019
Source
Escherichia Coli.
Synonyms
Pyroglutamyl-peptidase 1, EC 3.4.19.3, 5-oxoprolyl-peptidase, Pyroglutamyl aminopeptidase I, PAP-I, Pyroglutamyl-peptidase I, PGP-I, Pyrrolidone-carboxylate peptidase, PGPEP1, PGPI, PGP, Pcp.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PGPEP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209) and having a molecular mass of 25.5kDa.
PGPEP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Pyroglutamyl-Peptidase I (PGPEP1) is an omega peptidase responsible for cleaving pyroglutamyl residues from the N-terminus of peptides and proteins. Found in the cytosol of most cell types, this cysteine peptidase requires a thiol-reducing agent for activity. PGPEP1 is believed to play a role in inactivating biologically active peptides with an N-terminal pyroglutamyl group, such as neurotensin, luteinizing hormone-releasing hormone, and thyrotropin-releasing hormone.
Description
Recombinant human PGPEP1, expressed in E.coli, is a single, non-glycosylated polypeptide chain comprising 232 amino acids (1-209). It has a molecular weight of 25.5kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile filtered.
Formulation
The PGPEP1 solution is provided at a concentration of 1mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.15M NaCl, 20% glycerol, and 1mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 95.0% by SDS-PAGE analysis.
Synonyms
Pyroglutamyl-peptidase 1, EC 3.4.19.3, 5-oxoprolyl-peptidase, Pyroglutamyl aminopeptidase I, PAP-I, Pyroglutamyl-peptidase I, PGP-I, Pyrrolidone-carboxylate peptidase, PGPEP1, PGPI, PGP, Pcp.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEQPRKA VVVTGFGPFG EHTVNASWIA VQELEKLGLG DSVDLHVYEI PVEYQTVQRL IPALWEKHSP QLVVHVGVSG MATTVTLEKC GHNKGYKGLD NCRFCPGSQC CVEDGPESID SIIDMDAVCK RVTTLGLDVS VTISQDAGRY LCDFTYYTSL YQSHGRSAFV HVPPLGKPYN ADQLGRALRA IIEEMLDLLE QSEGKINYCH KH.

Product Science Overview

Structure and Source

The human recombinant form of PGPEP-1 is typically produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 232 amino acids . The recombinant enzyme is often tagged with a histidine tag to facilitate purification and detection . The molecular mass of the recombinant enzyme is approximately 24-26 kDa .

Function and Activity

PGPEP-1 is responsible for cleaving amino terminal pyroglutamate residues from protein substrates, including neuropeptides such as thyrotropin-releasing hormone . This activity is essential for the proper functioning and regulation of various biological processes. The enzyme requires a thiol-reducing agent for its activity, which helps maintain the cysteine residues in their reduced state .

Clinical Relevance

The expression and activity of PGPEP-1 have been studied in the context of various diseases. For instance, its expression may be downregulated in colorectal cancer, and its activity is negatively correlated with cancer progression in colorectal cancer patients . This suggests that PGPEP-1 could potentially serve as a biomarker for certain types of cancer.

Applications

Recombinant PGPEP-1 is widely used in research to study its enzymatic properties and potential therapeutic applications. It is also utilized in various biochemical assays to investigate the role of pyroglutamyl residues in protein function and stability .

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