Membrane Metalloendopeptidase Human Recombinant
This recombinant human MME protein is produced in Sf9 insect cells. It is a single, glycosylated polypeptide chain encompassing amino acids 52 to 750 of the MME protein sequence. This results in a protein with a molecular weight of 80.9 kDa. Note: On SDS-PAGE, the protein may appear between 70-100 kDa due to glycosylation. The recombinant protein is tagged with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.
Sf9, Insect cells.
Aminopeptidase Aeromonas Recombinant
Alanyl Aminopeptidase Membrane Mouse Recombinant
ANPEP Mouse, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain consisting of 943 amino acids (33-966 a.a.) with a molecular weight of 107.5 kDa. This recombinant protein is expressed with a 9 amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.
Aspartic Peptidase, Retroviral-Like 1 Human Recombinant
Carboxypeptidase-B Rat Recombinant
Caspase 2 Apoptosis-Related Cysteine Peptidase Human Recombinant
Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant
Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant, Sf9
This product consists of the human CASP3 protein produced using Sf9 insect cells infected with a baculovirus expression system. It is a single polypeptide chain that has undergone glycosylation, a common post-translational modification. The protein encompasses amino acids 29 to 277 of the CASP3 sequence, resulting in a protein of 256 amino acids. The molecular weight of the protein is 29.4 kDa. On SDS-PAGE analysis under reducing conditions, it migrates with an apparent molecular weight between 13.5 and 18 kDa. The protein has been engineered to include a 6-amino acid histidine tag at the C-terminus, facilitating its purification. Purification is achieved using proprietary chromatographic techniques.
ClpP Caseinolytic Peptidase Human Recombinant
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 has a molecular mass of 54.9 kDa. On SDS-PAGE, the molecular size will appear at approximately 50-70 kDa. This protein is expressed with an 8 amino acid His tag at the C-terminus and is purified by proprietary chromatographic techniques. |
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:
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.