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Validated All-in-One™ qPCR Primer for KHDRBS1(NM_006559.3) Search again
Product ID:
HQP168744
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
Sam68, p62, p68
Gene Description:
KH RNA binding domain containing, signal transduction associated 1
Target Gene Accession:
NM_006559.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Gene References into function
- Sam68 can cooperate with RNA helicase A and Tap to mediate the nuclear export of HIV-1 mRNA in the absence of Rev
- studies demonstrate that a lower level of constitutive Sam68 expression, followed by further down-regulation by HIV-1 infection, contributes to impaired Rev function in astrocytes and that Sam68 may play an important role in Rev nuclear export
- Down-modulation of Sam68 expression caused exclusive nuclear retention and colocalization of both Rev and CRM1.
- Here we describe the identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a protein that specifically interacts with Sam68 in vitro and in vivo.
- Sam68-mediated, HIV-1 RRE RNA-dependent gene expression is inhibited by heterogeneous nuclear ribonucleoprotein K (hnRNP K)
- the distinct potential of Fyn and Lck to phosphorylate Sam68 is likely controlled by the interaction of the kinase SH3 domain with the linker and Sam68, possibly on a competitive binding basis.
- Sam68 functioned to enhance the cytoplasmic utilization of RNA containing the CTE. These results suggest that Sam68 may interact with specific RNAs in the nucleus to provide a "mark" that affects their cytoplasmic fate
- tr-kit promotes the formation of a multimolecular complex composed of Fyn, PLCgamma1 and Sam68, which allows phosphorylation of PLCgamma1 by Fyn, and may modulate RNA metabolism.
- The participation of Sam68 in signaling suggests that it may function as an adaptor molecule, working as a dock to recruit other signaling molecules.
- Sam68 is involved in Rev-mediated RNA export and is required for HIV production.
- Sam68 suppresses BRK-induced cell proliferation, and regulates intranuclear localization and cell cycle progression
- Tyrosine 440 was identified as a principal modulator of Sam68 (KHDRBS1) localization to the nucleus and this site was phosphorylated in response to EGF treatment.
- Sam68 (KHDRBS1) is a positive regulator of adipocyte differentiation and a negative regulator of osteoblast differentiation in mice.
- shows Sam68 is modified by SUMO, and demonstrate that the SUMO E3 ligase (PIAS1) (protein inhibitor of activated STAT1) can enhance Sam68 sumoylation
- Results suggest that hsp22 specifically binds to Sam68 and modulates its activity, thus playing a role in the post-transcriptional regulation of gene expression.
- identified 23 mRNAs that are associated with the immunoprecipitated endogenous Sam68 protein complex. Five of the identified mRNAs were validated by co-immunoprecipitation assay followed by reverse transcription PCR
- Our results indicate that Sam68 plays a role in the regulation of Bcl-x alternative splicing and that tyrosine phosphorylation of Sam68 by Src-like kinases can switch its role from proapoptotic to antiapoptotic in live cells.
- The results suggest that the RG repeats conserved in Sam68 and SLM proteins may function as an auxiliary RNA binding domain and arginine methylation may eliminate or reduce an RNA binding ability of the proteins
- results strongly suggest that Sam68 contributes to transformation by oncogenic Vav1
- The signaling adaptor p62 is induced by Ras, its levels are increased in human tumors, and it is required for Ras-induced survival and transformation.
- The authors demonstrate that inhibition of HIV expression by Sam68DeltaC is correlated with a loss of PABP1 binding with no attendant change in polyadenosine tail length of the affected RNAs.
- Sam68 cytoplasmic mutants potently suppress Nef expression.
- Sam68 blocks HIV-1 structural protein synthesis.