Enzymes
Product List
MME Human
Membrane Metalloendopeptidase Human Recombinant
MME Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 a.a.) and having a molecular mass of 80.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
MME is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Aminopeptidase
Aminopeptidase Aeromonas Recombinant
ANPEP Mouse
Alanyl Aminopeptidase Membrane Mouse Recombinant
ANPEP Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 943 amino acids (33-966 a.a.) and having a molecular mass of 107.5 kDa. ANPEPis expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
ASPRV1 Human
Aspartic Peptidase, Retroviral-Like 1 Human Recombinant
ASPRV1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Carboxypeptidase B Rat
Carboxypeptidase-B Rat Recombinant
Recombinant Rat Carboxypeptidase-B is expressed in E.Coli having a Mw of 31kDa is purified by standard chromatography techniques.
Recombinant Rat Carboxypeptidase-B is free from foreign enzymes such as carboxypeptidase A & chymotrypsin. Recombinant Carboxypeptidase-B is free from protease inhibitors such as PMSF and EDTA.
CASP2 Human
Caspase 2 Apoptosis-Related Cysteine Peptidase Human Recombinant
CASP2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CASP3 Human
Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant
CASP3 is purified by proprietary chromatographic techniques.
CASP3 Human, Sf9
Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant, Sf9
CASP3 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (29-277 a.a.) and having a molecular mass of 29.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions).
CASP3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
FAP Human
Fibroblast Activation Protein Alpha Human Recombinant
FAP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 744 amino acids (26-760aa) and having a molecular mass of 86.1 kDa.
FAP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
GLU-C S.aureus
Glutamyl endopeptidase Staphylococcal 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.
