Rabbit Anti-SELENOS Recombinant Antibody (CBXS-0957) (CBMAB-S3868-CQ)

Rabbit

Human

CBXS-0957

IgG

WB, IP

Human

IgG

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Selenoprotein S

This gene encodes a transmembrane protein that is localized in the endoplasmic reticulum (ER). It is involved in the degradation process of misfolded proteins in the ER, and may also have a role in inflammation control. This protein is a selenoprotein, containing the rare amino acid selenocysteine (Sec). Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Two additional phylogenetically conserved stem-loop structures (Stem-loop 1 and Stem-loop 2) in the 3' UTR of this mRNA have been shown to function as modulators of Sec insertion. An alternatively spliced transcript variant, lacking the SECIS element and encoding a non-Sec containing shorter isoform, has been described for this gene (PMID:23614019).

Selenoprotein S; VCP-Interacting Membrane Protein; Valosin-Containing Protein-Interacting Membrane Protein; VCP Interacting Membrane Selenoprotein; VIMP; SELS;

Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination.

Biological Process cell redox homeostasisManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process cellular response to insulin stimulusManual Assertion Based On ExperimentTAS:BHF-UCL
Biological Process cellular response to lipopolysaccharideManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process cellular response to oxidative stressManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process endoplasmic reticulum unfolded protein responseManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process ER overload responseManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process establishment of protein localizationManual Assertion Based On ExperimentTAS:UniProtKB
Biological Process negative regulation of acute inflammatory response to antigenic stimulusManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathwayManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process negative regulation of glucose importManual Assertion Based On ExperimentTAS:BHF-UCL
Biological Process negative regulation of glycogen biosynthetic processManual Assertion Based On ExperimentTAS:BHF-UCL
Biological Process negative regulation of inflammatory response1 PublicationIC:BHF-UCL
Biological Process negative regulation of interleukin-6 productionISS:BHF-UCL
Biological Process negative regulation of macrophage apoptotic processManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process negative regulation of nitric-oxide synthase biosynthetic processManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process negative regulation of tumor necrosis factor productionISS:BHF-UCL
Biological Process regulation of gluconeogenesisManual Assertion Based On ExperimentTAS:BHF-UCL
Biological Process regulation of nitric oxide metabolic processManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process response to glucoseManual Assertion Based On ExperimentIEP:UniProtKB
Biological Process response to redox stateManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process retrograde protein transport, ER to cytosolManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process ubiquitin-dependent ERAD pathwayManual Assertion Based On ExperimentIDA:UniProtKB

Endoplasmic reticulum membrane
Cytoplasm

Helical: 28-48

Truncated SELENOS proteins produced by failed UGA/Sec decoding are ubiquitinated by the CRL2(KLHDC2) and CRL2(KLHDC3) complexes, which recognizes the glycine (Gly) at the C-terminus of truncated SELENOS proteins (PubMed:26138980, PubMed:30526872).
Truncated SELENOS proteins produced by failed UGA/Sec decoding are also ubiquitinated by the CRL5(KLHDC1) complex (PubMed:32200094).