SELM / Selenoprotein M Protein Price Inquiry ( Available Sizes )
SELM / Selenoprotein M Protein Product Information
A DNA sequence encoding the mature form of human SELM (Q8WWX9) (Ala 24-Leu 145) was fused with a polyhistidine tag at the C-terminus and an initial Met at the N-terminus.
SELM / Selenoprotein M Protein QC Testing
||> 97 % as determined by SDS-PAGE
SELM / Selenoprotein M protein
||Please contact us for more information.
||Samples are stable for up to twelve months from date of receipt at -70℃
|Predicted N terminal:
The recombinant human SELM comprises 133 amino acids and has a calculated molecular mass of 15.4KDa. It migrates as an approximately 19 kDa band d in SDS-PAGE under reducing conditions.
||Lyophilized from sterile 50mM Tris, 50mM NaCl, 50mM Arg, 0.3% Tween 20,5% glycerol; pH8.5.
- Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
- Please contact us for any concerns or special requirements.
SELM / Selenoprotein M Protein Usage Guide
||Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
||A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
SELM / Selenoprotein M Protein Related Products & Topics
SELM / Selenoprotein M Protein Description
Selenoprotein M is a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine M is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This gene is expressed in a variety of tissues, and the protein is localized to the perinuclear structures. Selenoprotein M May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation. This protein is widely expressed and is highly expressed in brain. It is found in Cytoplasm, perinuclear region, Endoplasmic reticulum, Golgi apparatus. Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum. Overexpression of Selenoprotein M resulted in a reduction in reactive oxygen species and apoptotic cell death in response to oxidative challenge with hydrogen peroxide. In contrast, knock-down of selenoprotein M using shRNA in primary neuronal cultures caused apoptotic cell death comparable to levels resulting from addition of hydrogen peroxide. Overexpression of selenoprotein M decreased calcium influx in response to hydrogen peroxide. Additionally, knock-down of selenoprotein M expression in cortical cultures caused higher baseline levels of cytosolic calcium than in control cells. These results suggest that selenoprotein M may have an important role in protecting against oxidative damage in the brain and may potentially function in calcium regulation.
- Reeves MA. et al., 2010, Antioxid Redox Signal. 12 (7): 809-18.
- Lu W. et al., 2012, Peptides. 34 (1): 168-76.
- García-Triana A. et al., 2010, Comp Biochem Physiol A Mol Integr Physiol. 155 (2): 200-4.