Mouse Interleukin-33

Product code: 32-12210

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  •   10 µg

  •  100 µg

  • $410.00 

  • $973.00 

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Amount : 100 µg
Purification : Reducing and Non-Reducing SDS PAGE at >= 90%
Content : Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM sodium phosphate, pH 7.5
Sterile water at 0.1 mg/mL
Storage condition : Store at -20°C
AA sequence : MSIQGTSLLT QSPASLSTYN DQSVSFVLEN GCYVINVDDS GKDQEQDQVL LRYYESPCPA SQSGDGVDGK KLMVNMSPIK DTDIWLHAND KDYSVELQRG DVSPPEQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEEKDESCN NIMFKLSKI
Gene : Il33
Gene ID : 77125
Uniprot ID : Q8BVZ5
Source: Genetically modified E.coli.
Predicted MW: Monomer, 17.7 kDa (159 aa)
Interleukin 33 (IL-33) is a member of the IL-1 cytokine family and is constitutively expressed in smooth muscle and airway epithelial cells.  IL-33 signals through the interleukin 1 receptor-like 1 (IL-1R1) and interleukin-1 receptor accessory protein (IL1RAP) receptors to ativate NF-kB and MAPK signaling pathways.  IL-33 functions to induce type 2 cytokine production in polarized Type 2 helper T (Th2) cells.  

Endotoxin: Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Biological Activity was determined by D10S cell proliferation at <=2 ng/mL; >= 5.0 x 10^5 units/mg (typical ED50 is < 1 ng/mL). Centrifuge vial before opening, Suspend the product by gently pipetting the above recommended solution down the sides of the vial. DO NOT VORTEX. Allow several minutes for complete reconstitution. For prolonged storage, dilute to working aliquots in a 0.1% BSA solution, store at -80°C and avoid repeat freeze thaws. Upon reconstitution, a small amount of visible precipitate can be expected. A 10% overfill has been added to the total material vialed to compensate for this loss.

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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