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The antibody against PRSS2 was raised in rabbit using the Recombinant Human Trypsin-2 protein (24-247AA) as the immunogen. This antibody exists as a hrp conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA.
The antibody against PRSS2 was raised in rabbit using the Recombinant Human Trypsin-2 protein (24-247AA) as the immunogen. This antibody exists as a hrp conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA.
$299.00
| Cat.No | ADC-13929A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | PRSS2 |
| Form | Liquid | Species Reactivity | Human |
| Isotype | IgG | Storage Buffer | 0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4 |
| Purification Method | >95%, Protein G purified | Conjugate | HRP conjugated |
| Application | ELISA | Storage | Upon receipt |
| Immunogen Description | Recombinant Human Trypsin-2 protein (24-247AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P07478 |
Uniprot Id
P07478
Target Species
Human
Target Name
PRSS2
Target Full Name
Trypsin-2
Target Function
In the ileum, may be involved in defensin processing, including DEFA5.
Target Subcellular Location
Secreted, extracellular space.
Target Protein Families
Peptidase S1 family
Target Tissue Specificity
Expressed in Paneth cells, at the base of small intestinal crypts.
Target Research Area
Cell Biology
Target Synonyms
(Anionic trypsinogen)(Serine protease 2)(Trypsin II)
Target Background
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.
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