Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human KHDRBS1 Protein expressed in Wheat germ - ABIN1308538
Lawrence, Schafer, Rieder: The nuclear protein Sam68 is cleaved by the FMDV 3C protease redistributing Sam68 to the cytoplasm during FMDV infection of host cells. in Virology 2012
Results revealed that upregulation of Sam68 significantly inhibited cisplatin-induced apoptosis in oral tongue squamous cell carcinoma cells.
The PRMT2 (show PRMT2 Proteins) interacts with SAM68 in cells and regulates its subcellular localization via the SH3 domain of PRMT2 (show PRMT2 Proteins), prompting us to investigate the potential role of PRMT2 (show PRMT2 Proteins) in BCL-X (show BCL2L1 Proteins) alternative splicing.
Data suggest that the first 22 bp of exon 3 in BIRC5 (show BIRC5 Proteins) contain cis (show CISH Proteins)-acting elements that enhance the exclusion of exon 3 to generate the survivin (show BIRC5 Proteins) DEx3 mRNA isoform via exclusion/deletion of exon 3; Sam68 is a possible trans-acting factor that binds to this cis (show CISH Proteins)-acting element and regulates exon 3 splicing. (BIRC5/survivin (show BIRC5 Proteins) = baculoviral IAP repeat containing 5 (show BIRC5 Proteins); Sam68 = GAP-associated tyrosine phosphoprotein p62)
our results indicated that Sam68 modulates apoptosis of intestinal epithelial cells via mediating NF-kappaB (show NFKB1 Proteins) activation in ulcerative colitis
Sam68 possibly participated in the progresses of T-acute lymphoblastic leukemia at least partially via AKT (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) signaling pathway
Sam68 is essential for DNA damage-induced NF-kappaB (show NFKB1 Proteins) activation and colon tumorigenesis.
These findings define a hitherto novel mechanism of action for Sam68 in governing p53 (show TP53 Proteins) transcriptional activation, and represent the first report of Sam68 in the regulation of tumor suppressor activities.
HNRNPL (show HNRNPL Proteins) acts as the adaptor to combine the two substructures and form the intact Sam68 nuclear body through the interaction of two sets of RNA recognition motifs with the putative architectural RNA in the respective substructures.
Sam68 was overexpressed in EOC tissue in association with such cancer malignant factors of FIGO stage, histological grade, and lymph node metastasis, and also positively regulated the proliferation of EOC cells.
Taken together, these results illuminated that enterovirus 71 infections can induce stress granule formation, and Sam68, as a stress granule component, migrates alone with stress granules dependent on intact microtubule upon the viral infections.
Sam68-haploinsufficiency significantly delayed the onset of tumors in mice lacking p53 (show TP53 Proteins) and prolonged their survival, indicating that Sam68 accelerates the development of p53 (show TP53 Proteins)-deficient tumors.
Sam68 deletion diminishes gamma-irradiation-triggered PAR (show AFG3L2 Proteins) synthesis and NF-kappaB (show NFKB1 Proteins) activation in colon epithelial cells (CECs), thus hampering the expression of anti-apoptotic molecules in situ and facilitating CECs to undergo apoptosis in mice post whole-body gamma-irradiation (WBIR).
This study identifies Sam68 as a key regulator of neural progenitor cell self-renewal and establishes a novel link between modulation of ALDH1A3 (show ALDH1A3 Proteins) expression and maintenance of high glycolytic metabolism in the developing cortex.
Sam68 may function as an immune rheostat that balances the activation of NF-kappaB (show NFKB1 Proteins) p65 (show NFkBP65 Proteins) and c-Rel (show NFkBP65 Proteins), as well as MAPK (show MAPK1 Proteins), revealing a potential novel target to manipulate TLR signaling.
Sam68 plays a crucial role in DNA damage response via regulating DNA damage-initiated PAR (show AFG3L2 Proteins) production.
Sam68 and T-STAR could regulate alternative splicing of some pre-mRNAs by bringing two distant UAA motifs into proximity and looping out regions of the pre-mRNA.
SAM68 is a physiological regulator of SMN2 (show SMN1 Proteins) splicing in a spinal muscular atrophy mouse model.
Data (including data from knockout mice) suggest expression of Sam68 plays role in adipogenesis of white adipose tissue versus brown adipose tissue; Sam68 appears to regulate adiposity and energy homeostasis (balance of energy intake/expenditure).
This gene encodes a member of the K homology domain-containing, RNA-binding, signal transduction-associated protein family. The encoded protein appears to have many functions and may be involved in a variety of cellular processes, including alternative splicing, cell cycle regulation, RNA 3'-end formation, tumorigenesis, and regulation of human immunodeficiency virus gene expression. Alternative splicing results in multiple transcript variants.
GAP-associated tyrosine phosphoprotein p62 (Sam68)
, KH domain-containing, RNA-binding, signal transduction-associated protein 1
, p21 Ras GTPase-activating protein-associated p62
, src-associated in mitosis 68 kDa protein
, GAP-associated phosphoprotein p62
, KH domain containing, RNA binding, signal transduction associated 1
, GAP-associated tyrosine phosphoprotein p62
, src associated in mitosis, 68 kDa
, KH domain RNA-binding protein Sam68