Growth Factors
CD Antigens
Enzymes
Viral Antigens
Recombinant Proteins
Natural Proteins
Monoclonal Antibodies
Cytokines
Polyclonal Antibodies
Neurotrophins
Chemokines
Hormones
Custom Antibodies
Modified Histone Antibodies
Tag/Control Antibodies
Antibody Pairs
Secondary Antibodies
Small Molecular Antibodies
Recombinant Antibodies
ChIP Antibodies
Enzymes
Product List
PRSS7 Human
Protease Serine 7 Human Recombinant
Recombinant human PRSS7, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 237 amino acids (residues 785-1019). This protein has a molecular weight of 26.4 kDa. The purification of PRSS7 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT4611
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
BACE1 Human
Beta-Secretase 1 Human Recombinant
This product consists of human BACE1, produced in Sf9 insect cells using a baculovirus expression system. It is a single, glycosylated polypeptide chain with a molecular weight of 49.2 kDa. The recombinant protein encompasses amino acids 22-457 and includes a 6-amino acid His tag at the C-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT3608
Source
Sf9,
Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.
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 and having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at the C-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
IDE Human
Insulin-Degrading Enzyme Human Recombinant
Recombinant human IDE, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 1026 amino acids. This includes the 1019 amino acids of IDE (Met1-Leu1019) and a 7 amino acid His tag located at the C-terminus. The calculated molecular mass of the protein is 119kDa.
Shipped with Ice Packs
Cat. No.
BT3748
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been filtered.
IDE Human, Active
Insulin-Degrading Enzyme Human Recombinant
IDE Human, Active is a recombinant human Insulin Degrading Enzyme produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of amino acids 42-1019 (total 984 amino acids) and has a molecular mass of 114 kDa. This protein includes a 6-amino acid His-tag at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
LGMN Human
Legumain Human Recombinant
LGMN, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain encompassing amino acids 18 to 433. It is fused to a 6 amino acid His Tag at the C-terminus, resulting in a total of 422 amino acids and a molecular mass of 48.4 kDa. On SDS-PAGE, the molecular size will appear approximately between 40-57 kDa. The purification of LGMN is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3897
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution that has been sterilized by filtration.
Introduction
Definition and Classification
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.
Biological Properties
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.
Biological Functions
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.
Modes of Action
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
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.
Applications
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 in the Life Cycle
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.
