Enzymes
Product List
BACE1 Human
Beta-Secretase 1 Human Recombinant
BACE1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 442 amino acids (22-457 a.a.) and having a molecular mass of 49.2kDa. BACE1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
BACE2 Mouse, HEK
Beta-Secretase 2 Mouse Recombinant, HEK
BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa.
BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
IDE Human
Insulin-Degrading Enzyme Human Recombinant
IDE Human, Active
Insulin-Degrading Enzyme Human Recombinant
IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa.
IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
LGMN Human
Legumain Human Recombinant
LGMN is purified by proprietary chromatographic techniques.
LGMN Mouse
Legumain Mouse Recombinant
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Protease
Recombinant Protease
The Recombinant Protease is purified by proprietary chromatographic techniques.
PRSS22 Mouse
Protease Serine 22 Mouse Recombinant
PRSS22 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
PRSS28 Mouse
Protease Serine 28 Mouse Recombinant
PRSS3 Human
Protease Serine 3 Human Recombinant
Introduction
Proteases, also known as peptidases or proteinases, are enzymes that catalyze the hydrolysis of peptide bonds in proteins. They play a crucial role in various biological processes by breaking down proteins into smaller peptides or amino acids. Proteases are classified based on their catalytic mechanism into several categories:
- Serine proteases: Utilize a serine residue in their active site.
- Cysteine proteases: Employ a cysteine residue for catalysis.
- Aspartic proteases: Use an aspartic acid residue.
- Metalloproteases: Require a metal ion, usually zinc, for activity.
- Threonine proteases: Utilize a threonine residue in their active site.
Key Biological Properties:
- Catalytic Activity: Proteases exhibit high specificity for their substrates, ensuring precise cleavage of peptide bonds.
- Stability: They are stable under various physiological conditions, including different pH levels and temperatures.
Expression Patterns and Tissue Distribution:
- Proteases are ubiquitously expressed in all living organisms, from bacteria to humans.
- They are found in various tissues, including the digestive tract, blood, and immune cells.
- Specific proteases are localized in particular cellular compartments, such as lysosomes, mitochondria, and the extracellular matrix.
Primary Biological Functions:
- Protein Digestion: Proteases break down dietary proteins into absorbable amino acids.
- Cellular Regulation: They regulate cellular processes by activating or degrading key proteins.
- Apoptosis: Proteases like caspases play a vital role in programmed cell death.
Role in Immune Responses and Pathogen Recognition:
- Proteases are involved in the activation of immune cells and the processing of antigens for presentation to the immune system.
- They help in the recognition and elimination of pathogens by degrading their proteins.
Mechanisms with Other Molecules and Cells:
- Proteases interact with substrates through their active sites, where they catalyze the cleavage of peptide bonds.
- They can form complexes with inhibitors or activators that modulate their activity.
Binding Partners and Downstream Signaling Cascades:
- Proteases often bind to specific inhibitors that regulate their activity, such as serpins for serine proteases.
- They can initiate downstream signaling cascades by cleaving and activating other proteins, such as in the blood coagulation pathway.
Regulatory Mechanisms Controlling Expression and Activity:
- Transcriptional Regulation: Protease gene expression is controlled by transcription factors that respond to cellular signals.
- Post-Translational Modifications: Proteases can be activated or inhibited by modifications such as phosphorylation, glycosylation, and ubiquitination.
Biomedical Research:
- Proteases are used to study protein function and structure by selectively cleaving target proteins.
Diagnostic Tools:
- Protease activity assays are employed in diagnostic tests for diseases such as cancer and infectious diseases.
Therapeutic Strategies:
- Protease inhibitors are used as drugs to treat conditions like hypertension, HIV, and cancer.
Role Throughout the Life Cycle:
- Development: Proteases are essential for tissue remodeling and organ development.
- Aging: Changes in protease activity are associated with aging and age-related diseases.
- Disease: Dysregulation of protease activity is linked to various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases.
