Recombinant Proteins
Product List
Trypsin Bovine
Trypsin Bovine Recombinant
Recombinant Bovine Trypsin is free from any animal and human sources. Trypsin Bovine specifically cleaves peptide bonds after basic amino acids such as lysine and arginine.
Trypsin Porcine
Trypsin Porcine Recombinant
Recombinant Porcine Trypsin is expressed in E.coli and purified by standard chromatography techniques.
Trypsin-2 Human
Trypsin-2 Human Recombinant
Recombinant Human Trypsin-2 expressed in E.Coli having an Mw of 24kDa is purified by standard chromatography techniques.
Introduction
Key Biological Properties: Trypsin is produced in the pancreas as an inactive precursor called trypsinogen. Upon entering the small intestine, trypsinogen is activated into trypsin by the enzyme enterokinase . Trypsin exhibits remarkable specificity, cleaving peptide bonds at the carboxyl side of lysine or arginine residues .
Expression Patterns and Tissue Distribution: Trypsin is predominantly expressed in the pancreas and is secreted into the small intestine. It is also found in other tissues, including the digestive system of many vertebrates .
Primary Biological Functions: The primary function of trypsin is to catalyze the hydrolysis of peptide bonds, aiding in the digestion of proteins into smaller peptides and amino acids. This process is essential for protein absorption in the small intestine .
Role in Immune Responses and Pathogen Recognition: Trypsin has been implicated in various immune responses, including the activation of other proteases and the modulation of immune cell functions. It also plays a role in pathogen recognition and defense mechanisms .
Mechanisms with Other Molecules and Cells: Trypsin interacts with other molecules and cells through its catalytic activity. It activates other proteases, such as chymotrypsin and carboxypeptidase, by proteolytic cleavage .
Binding Partners and Downstream Signaling Cascades: Trypsin binds to specific substrates and cleaves peptide bonds, leading to the activation of downstream signaling cascades. These cascades are involved in various physiological processes, including digestion and immune responses .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of trypsin are tightly regulated. Trypsinogen is activated into trypsin by enterokinase in the small intestine. Additionally, trypsin can activate more trypsinogen, creating a positive feedback loop .
Transcriptional Regulation and Post-Translational Modifications: The transcription of trypsinogen is regulated by various factors, including hormones and signaling molecules. Post-translational modifications, such as phosphorylation and glycosylation, also play a role in regulating trypsin activity .
Biomedical Research: Trypsin is widely used in biomedical research, particularly in proteomics, where it is used to digest proteins into peptides for mass spectrometry analysis .
Diagnostic Tools: Trypsin levels are measured in diagnostic tests for conditions such as pancreatitis and cystic fibrosis .
Therapeutic Strategies: Trypsin has therapeutic applications in wound healing, where it helps remove necrotic tissue and promotes healthy tissue growth. It also has anti-inflammatory properties and is used in the treatment of burns, ulcers, and skin infections .
Role Throughout the Life Cycle: Trypsin plays a vital role throughout the life cycle, from development to aging and disease. It is essential for protein digestion and nutrient absorption, which are critical for growth and development. Altered trypsin activity has been associated with various diseases, including cancer and metabolic disorders .
