Enzymes
Product List
OSGEP Human
O-Sialoglycoprotein Endopeptidase Human Recombinant
PCOLCE Human
Procollagen C-Endopeptidase Enhancer Human Recombinant
PCOLCE Human, Sf9
Procollagen C-Endopeptidase Enhancer Human Recombinant, Sf9
PCOLCE produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 433 amino acids (26-449 a.a.) and having a molecular mass of 46.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
PCOLCE is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Insect cells.
PEPD Human
Peptidase D Human Recombinant
PEPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PGPEP1 Human
Pyroglutamyl-Peptidase I Human Recombinant
PGPEP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PI16 Human
Peptidase Inhibitor 16 Human Recombinant
The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.
PRCP Human
Prolylcarboxypeptidase Human Recombinant
PRCP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-496 a.a) containing a total of 481 amino acids, having a molecular mass of 54.3 kDa.
PRCP is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
PREP Human
Prolyl Endopeptidase Human Recombinant
SENP8 Human
Sentrin Specific Peptidase Family Member 8 Human Recombinant
SENP8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.2 kDa.
The SENP8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
SERPINE2 Mouse
Plasminogen Activator Inhibitor-2 Mouse Recombinant
SERPINE2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 386 amino acids (20-397a.a.) and having a molecular mass of 42.9kDa. SERPINE2 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Introduction
Peptidases, also known as proteases or proteinases, are enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes by breaking down proteins into smaller peptides or amino acids. Peptidases are classified based on their catalytic mechanisms and substrate specificities into several major groups:
- Serine peptidases: Utilize a serine residue in their active site.
- Cysteine peptidases: Contain a cysteine residue in their active site.
- Aspartic peptidases: Use an aspartic acid residue for catalysis.
- Metallopeptidases: Require a metal ion, usually zinc, for their activity.
- Threonine peptidases: Utilize a threonine residue in their active site.
Key Biological Properties: Peptidases exhibit high specificity for their substrates, ensuring precise cleavage of peptide bonds. They are involved in protein turnover, processing, and degradation. Expression Patterns: Peptidases are expressed in various tissues and cells, with specific peptidases being more abundant in certain tissues. Tissue Distribution: For example, digestive peptidases like trypsin and chymotrypsin are predominantly found in the pancreas, while lysosomal peptidases like cathepsins are abundant in lysosomes of various cell types.
Primary Biological Functions: Peptidases are essential for protein digestion, cellular protein turnover, and the activation of precursor proteins. Role in Immune Responses: They play a critical role in antigen processing and presentation, aiding the immune system in recognizing and responding to pathogens. Pathogen Recognition: Certain peptidases are involved in the degradation of pathogen-derived proteins, facilitating the immune response.
Mechanisms with Other Molecules and Cells: Peptidases interact with various substrates, inhibitors, and cofactors to regulate their activity. Binding Partners: They often form complexes with other proteins or molecules to enhance or inhibit their function. Downstream Signaling Cascades: Peptidase activity can trigger downstream signaling pathways, influencing cellular responses such as apoptosis, proliferation, and differentiation.
Expression and Activity Control: Peptidase expression is tightly regulated at the transcriptional level by various transcription factors and signaling pathways. Transcriptional Regulation: Specific genes encoding peptidases are activated or repressed in response to cellular signals. Post-Translational Modifications: Peptidases undergo modifications such as phosphorylation, glycosylation, and ubiquitination, which can alter their activity, stability, and localization.
Biomedical Research: Peptidases are studied for their roles in diseases such as cancer, neurodegenerative disorders, and infectious diseases. Diagnostic Tools: Peptidase activity assays are used in diagnostics to detect abnormalities in enzyme function. Therapeutic Strategies: Inhibitors of specific peptidases are developed as drugs to treat conditions like hypertension, cancer, and viral infections.
Development to Aging and Disease: Peptidases are involved in various stages of the life cycle, from embryonic development to aging. They play roles in tissue remodeling, cell differentiation, and apoptosis. Dysregulation of peptidase activity is associated with aging and various diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders.
