Detects human Trypsin 3/PRSS3 in Western blots. In Western blots, no cross-reactivity with recombinant human (rh) Trypsin-1 or rhTrypsin-2 is observed.
Monoclonal Rat IgG2A Clone # 420025
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human Trypsin 3/PRSS3 Val16-Ser247 Accession # NP_002762
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize Recombinant Human Active Trypsin 3/PRSS3 (0.03 µg/mL, Catalog # 3714-SE) cleavage of the fluorogenic peptide substrate Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (10 µM, Catalog # ES002). The Neutralization Dose (ND50) is typically 0.15 µg/mL.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Neutralization of Trypsin 3/ PRSS3 Activity by Human Trypsin 3/PRSS3 Antibody.
The cleavage of Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (10 µM, Catalog # ES002) by Recombinant Human Active Trypsin 3/PRSS3 (0.03 µg/mL, Catalog # 3714-SE) is measured after preincubation with increasing concentrations of Rat Anti-Human Trypsin 3/PRSS3 Monoclonal Antibody (Catalog # MAB3710). The ND50 is typically 0.15 µg/mL.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Trypsin 3/PRSS3
Trypsin 3, encoded by the PRSS3 gene, is also known as mesotrypsin (1).
Constituting less than 10% of the total trypsin content in normal
pancreatic juice, it is one of the three trypsin isoforms produced by
the pancreas (2). Compared to trypsin 1 and 2, one intriguing feature of
Trypsin 3 is its resistance to polypeptide trypsin inhibitors, such as
the Kunitz-type soybean trypsin inhibitor or the Kazal-type pancreatic
secretory trypsin inhibitor. As revealed by the crystal structure, this
resistance is likely due to the presence of an arginine residue in place
of the highly conserved Gly198 (3). Trypsin 3 is synthesized
in the pancreas and secreted into the duodenum lumen, where it is
activated by enterokinase. One proposed physiological function of
Trypsin 3 is degradation of trypsin inhibitors, which facilitates the
digestion of those foods rich in these proteins (4).
Nyaruhucha, C. N. M. et al. (1997) J. Biol. Chem. 272:10573.
Rinderknecht, H. et al. (1984) Gastroenterology 86:681.
Katona, G. et al. (2002) J. Mol. Biol. 315:1209.
Szmola, R. et al. (2003) J. Biol. Chem. 278:48580.
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