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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. Additionally we are shipping SECIS Binding Protein 2 Kits (2) and and many more products for this protein.
Showing 10 out of 63 products:
Human Polyclonal SECISBP2 Primary Antibody for IP, IHC - ABIN185714
Papp, Lu, Striebel, Kennedy, Holmgren, Khanna: The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function. in Molecular and cellular biology 2006
Show all 3 references for ABIN185714
Human Polyclonal SECISBP2 Primary Antibody for EIA, WB - ABIN954708
Méplan, Hughes, Pardini, Naccarati, Soucek, Vodickova, Hlavatá, Vrána, Vodicka, Hesketh: Genetic variants in selenoprotein genes increase risk of colorectal cancer. in Carcinogenesis 2010
Show all 2 references for ABIN954708
Human Polyclonal SECISBP2 Primary Antibody for ICC, IF - ABIN251681
Papp, Wang, Kennedy, Boucher, Zhang, Gladyshev, Singh, Khanna: Functional characterization of alternatively spliced human SECISBP2 transcript variants. in Nucleic acids research 2008
Show all 2 references for ABIN251681
Secisbp2 is essential for embryonic development and enhances selenoprotein expression.
SBP2/SECIS complex activates eEFSec by directing functional interactions between Domain IV and the ribosome to promote Sec-tRNA(Sec) binding and accommodation into the ribosomal A-site
Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.
Swapping only five amino acids between dSBP2 and human SBP2 in the K-rich domain conferred reversed SECIS-binding properties to the proteins, thus unveiling an important sequence for form 1 binding.
SBP2 makes direct contacts with a discrete region of the human 28S rRNA.
The patient showed typical symptoms of SBP2 deficiency, and novel compound heterozygous mutations were identified in SBP2 (p.M515fsX563/p.Q79X).
Describe subjects with compound heterozygous defects in the SECISBP2 gene. These individuals have reduced synthesis of most of the 25 known human selenoproteins, resulting in a complex phenotype.
Results demonstrate that SECIS-binding protein 2 is required for protection against reactive oxygen species-induced cellular damage and cell survival.
In addition to identifying key amino acids for SECIS recognition by SBP2, our findings led to the proposal that some of the recognition principles governing the 15.5 kD-U4 snRNA interaction must be similar in the SBP2-SECIS RNA complex
Oxidative stress induces nuclear accumulation of SBP2 via oxidation of cysteine residues within a redox-sensitive cysteine-rich domain.
Data suggest that SBP2 is a major determinant in dictating the hierarchy of selenoprotein synthesis via differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay.
SECIS binding induces a conformational change in SBP2 that recruits eEFSec (show EEFSEC Antibodies), which in concert with the Sec incorporation domain gains access to the ribosomal A site
A report of a complex splicing pattern in the 5'-region of human SECISBP2, wherein at least eight splice variants encode five isoforms with varying N-terminal sequence.
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.
selenocysteine insertion sequence-binding protein 2
, SECIS binding protein 2
, selenocysteine insertion sequence-binding protein 2-like
, SECIS-binding protein 2