SELM / Selenoprotein M抗体

SELM / Selenoprotein M抗体产品信息免疫原 : Recombinant Human SELM / Selenoprotein M protein (Catalog#13508-H08E)
Antibody Type : Rabbit Polyclonal Antibody ( Antibody Purification Platform )
抗体宿主 : Rabbit IgG
缓冲液 : 0.2 μm filtered solution in PBS, 5% trehalose may be added in some batches. Please read the hardcopy of COA or contact our customer service to confirm the formulation.
制备方法 : Produced in rabbits immunized with purified, recombinant Human SELM / Selenoprotein M (rh SELM / Selenoprotein M; Catalog#13508-H08E; Q8WWX9; Ala24-Leu145). SELM / Selenoprotein M specific IgG was purified by Human SELM / Selenoprotein M affinity chromatography.
SELM / Selenoprotein M抗体 Background
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.
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