ELISA kits are commonly used to measure soluble biomarkers across a variety of research areas. ELISA kits for Human Trypsin 2 can be quantified in various samples, including plasma, serum, supernatant.
Invitrogen ELISA kits exist in two formats: Uncoated and Coated....ELISA kits are commonly used to measure soluble biomarkers across a variety of research areas. ELISA kits for Human Trypsin 2 can be quantified in various samples, including plasma, serum, supernatant.
Invitrogen ELISA kits exist in two formats: Uncoated and Coated....ELISA kits are commonly used to measure soluble biomarkers across a variety of research areas. ELISA kits for Human Trypsin 2 can be quantified in various samples, including plasma, serum, supernatant.
Invitrogen ELISA kits exist in two formats: Uncoated and Coated. Uncoated ELISA kits include all the necessary reagents to coat your own plates and run your assay with maximum flexibility. Coated ELISA kits...
ELISA kits are commonly used to measure soluble biomarkers across a variety of research areas. ELISA kits for Human Trypsin 2 can be quantified in various samples, including plasma, serum, supernatant.
Invitrogen ELISA kits exist in two formats: Uncoated and Coated. Uncoated ELISA kits include all the necessary reagents to coat your own plates and run your assay with maximum flexibility. Coated ELISA kits are ready-to-use and quality tested for sensitivity, specificity, precision and lot-to-lot consistency.
靶标信息
This gene belongs to the trypsin family of serine proteases and encodes anionic trypsinogen. It is part of a cluster of trypsinogen genes that are located within the T cell receptor beta locus. Enzymes of this family cleave peptide bonds that follow lysine or arginine residues. This protein is found at high levels in pancreatic juice and its upregulation is a characteristic feature of pancreatitis. This protein has also been found to activate pro-urokinase in ovarian tumors, suggesting a function in tumor invasion. In addition, this enzyme is able to cleave across the type II collagen triple helix in rheumatoid arthritis synovitis tissue, potentially participating in the degradation of type II collagen-rich cartilage matrix. Alternative splicing results in multiple transcript variants.