|Application ||WB, IHC, IF, IP, ICC, E|
|Other Accession||NP_076982, 79048|
|Predicted||Pig, Dog, Cow|
|Calculated MW||95462 Da|
|Other Names||Selenocysteine insertion sequence-binding protein 2, SECIS-binding protein 2, SECISBP2, SBP2|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-SBP2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB.|
|Cellular Location||Isoform 1: Nucleus.|
|Tissue Location||Expressed at high levels in testis.|
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Provided below are standard protocols that you may find useful for product applications.
The incorporation of selenocysteine into a protein requires the concerted action of an mRNA element called a sec insertion sequence (SECIS), a selenocysteine-specific translation elongation factor and a SECIS binding protein. With these elements in place, a UGA codon can be decoded as selenocysteine. The gene described in this record encodes a nuclear protein that functions as a SECIS binding protein. Mutations in this gene have been associated with a reduction in activity of a specific thyroxine deiodinase, a selenocysteine-containing enzyme, and abnormal thyroid hormone metabolism.
Genetic variants in selenoprotein genes increase risk of colorectal cancer. M茅plan C, et al. Carcinogenesis, 2010 Jun. PMID 20378690.
SECIS-binding protein 2 promotes cell survival by protecting against oxidative stress. Papp LV, et al. Antioxid Redox Signal, 2010 Apr 1. PMID 19803747.
Clinical and molecular characterization of a novel selenocysteine insertion sequence-binding protein 2 (SBP2) gene mutation (R128X). Di Cosmo C, et al. J Clin Endocrinol Metab, 2009 Oct. PMID 19602558.
SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. Oli茅ric V, et al. Biochimie, 2009 Aug. PMID 19467292.
Selenium supplementation fails to correct the selenoprotein synthesis defect in subjects with SBP2 gene mutations. Schomburg L, et al. Thyroid, 2009 Mar. PMID 19265499.
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