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| Cat.No | ACP08373 | Target Name | PRSS8 |
|---|---|---|---|
| Target Synonyms | PRSS8; Prostasin; Channel-activating protease 1; CAP1; Serine protease 8 | Form | Lyophilized powder |
| Expression System | Custom Production. Please inquire and provide the desire expression system. | Protein Length | Partial |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q16651 |
|---|
Uniprot Id
Q16651
Target Species
Human
Target Name
PRSS8
Target Full Name
Prostasin
Target Function
Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G).
Target Subcellular Location
[Prostasin]: Cell membrane; Single-pass membrane protein.; [Prostasin light chain]: Secreted, extracellular space. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus.; [Prostasin heavy chain]: Secreted, extracellular space. Note=Found in the seminal fluid. Secreted after cleavage of its C-terminus.
Target Protein Families
Peptidase S1 family
Target Tissue Specificity
Found in prostate, liver, salivary gland, kidney, lung, pancreas, colon, bronchus and renal proximal tubular cells. In the prostate gland it may be synthesized in epithelial cells, secreted into the ducts, and excreted into the seminal fluid.
Target Synonyms
PRSS8; Prostasin; Channel-activating protease 1; CAP1; Serine protease 8
Target Background
This gene encodes a member of the peptidase S1 or chymotrypsin family of serine proteases. The encoded preproprotein is proteolytically processed to generate light and heavy chains that associate via a disulfide bond to form the heterodimeric enzyme. This enzyme is highly expressed in prostate epithelia and is one of several proteolytic enzymes found in seminal fluid. This protease exhibits trypsin-like substrate specificity, cleaving protein substrates at the carboxyl terminus of lysine or arginine residues. The encoded protease partially mediates proteolytic activation of the epithelial sodium channel, a regulator of sodium balance, and may also play a role in epithelial barrier formation.
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