Recombinant Mouse Interleukin-33/PRSS8 (C-Fc)(Discontinued)

Product code: 32-7613

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Amount : 50 µg
Content : Supplied as a 0.2 µm filtered solution of PBS,pH7.4.
Storage condition : Store at -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
AA sequence : ADGTEASCGAVIQPRITGGGSAKPGQWPWQVSITYDGNHVCGGSLVSNKWVVSAAHCFPREHSREAYEVKLGAHQLDSYSNDTVVHTVAQIITHSSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLQTPRPLQQLEVPLISRETCSCLYNINAVPEEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHHHVAELQVDDIEGRMDEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Gene : Il33
Gene ID : 77125
Uniprot ID : Q99L46
Source: Human Cells.
MW :55kD.
Recombinant Mouse Prostasin is produced by our Mammalian expression system and the target gene encoding Ala30-Gln289 is expressed with a Fc tag at the C-terminus. Prostasin also known as channel activating protease 1 (CAP1), is a trypsinlike serine peptidase, and plays important roles in epithelial physiology. Mouse Prostasin is found in the seminal fluid and secreted after cleavage of its C-terminus. Prostasin is found to activate the epithelial sodium channel (ENaC) which is regulated and is critical for maintaining salt and fluid balance in the lung and kidney in both normal and pathological conditions. Accordingly, prostasin has been proposed as a target for therapeutic inhibition in cystic fibrosis. In addition, prostasin inhibits prostate and breast cancer cell invasion in vitro, suggesting a functional role as a suppressor of tumor invasion, as well as a regulator of gene expression during inflammation.

Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Subcellular location: Nucleus, Chromosome, Cytoplasmic vesicle, Secreted
Post transnational modification: The full-length protein can be released from cells and is able to signal via the IL1RL1/ST2 receptor. However, proteolytic processing by CSTG/cathepsin G and ELANE/neutrophil elastase produces C-terminal peptides that are more active than the unprocessed full-length protein. May also be proteolytically processed by calpains. Proteolytic cleavage mediated by apoptotic caspases including CASP3 and CASP7 results in IL33 inactivation. In vitro proteolytic cleavage by CASP1 was reported (PubMed:16286016) but could not be confirmed in vivo (PubMed:19465481) suggesting that IL33 is probably not a direct substrate for that caspase.
BioGrid: 218533. 1 interactions.
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