Enteropeptidase
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Enteropeptidase
Description:
Enteropeptidase/Enterokinase initiates activation of pancreatic proteases by converting trypsinogen to trypsin, which in turn activates chymotrypsin, carboxypeptidases and elastases. Located in intestinal brush border, it is a disulfide bond linked dimer of the heavy and light chains, which are derived from the same single-chain precursor. The multi-domain-containing the heavy chain consists of a short cytoplasmic tail, a transmembrane, a SEA, a SRCR, a MAM, two CUB and two LDL-receptor class A domains. The light chain contains the catalytic domain of trypsin-like serine proteases.Synonyms:
TMPRSS15; ENTK; PRSS7; Enterokinase; Serine protease 7; Transmembrane protease serine 15NCBI Gene ID:
5651UniProt:
P98073Accession Number:
NP_002763.2Accession Number mRNA:
NM_002772.2Chromosomal Location:
21q21.1Reactivity:
Anti-HumanCross Reactivity:
HumanTarget Antigen:
Human recombinant Enteropeptidase (also called Enterokinase)Clone:
(#8S12)Applications:
WBPurification Method:
Protein G chromatographyAssay Protocol:
Centrifuge vial prior to opening. Reconstitute the antibody with 500 µl sterile PBS and the final concentration is 200 µg/ml.Bioactivity:
Western Blot: Use at 250 ng/ml-1 µg/mlForm:
LyophilizedBuffer:
PBSReconstitution:
PBSStorage Conditions:
Lyophilized samples are stable for 2 years from date of receipt when stored at -70°C. Reconstituted antibody can be aliquoted and stored frozen at < -20°C for at least six months without detectable loss of activity.Host or Source:
MouseIsotype:
IgG2
Related Products
CAT | Name |
|---|---|
| 101-M388 | Enteropeptidase |
