Enzymes
Product List
SPINK1 Human
Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant
SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
XPNPEP1 Human
X-Prolyl Aminopeptidase-1 Human Recombinant
CLPP Human
ClpP Caseinolytic Peptidase Human Recombinant
CLPP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (57-277 a.a.) and having a molecular mass of 24.2kDa.
CLPP is purified by proprietary chromatographic techniques.
CNDP1 Human
CNDP Dipeptidase 1 Human Recombinant
|
CNDP1 produced in Sf9
Insect cells is a single, glycosylated polypeptide chain containing 489 amino
acids (27-507a.a.) and having a molecular mass of 54.9kDa. (Molecular size on
SDS-PAGE will appear at approximately 50-70kDa). CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques. |
CNDP1 Human, Active
CNDP Dipeptidase 1 Human Recombinant, Active
CNDP1 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
CNDP1 Mouse
CNDP Dipeptidase 1 Mouse Recombinant
CNDP2 Human
CNDP Dipeptidase 2 Human Recombinant
CPA4 Human
Carboxypeptidase A4 Human Recombinant
CPA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (17-421a.a.) and having a molecular mass of 46.6kDa.
CPA4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
CPE Human
Carboxypeptidase-E Human Recombinant
DESI1 Human
Desumoylating Isopeptidase 1 Human Recombinant
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.
