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SIRT7 encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Additionally we are shipping Sirtuin 7 Antibodies (149) and Sirtuin 7 Kits (19) and many more products for this protein.
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Our data confirmed that SIRT7 was overexpressed in cholangiocarcinoma patient tissues and cell lines.
SIRT7 is involved in regulating TGF-beta1 (show TGFB1 Proteins)-induced ASM (show SMPD1 Proteins) cell proliferation.
Overexpression of SIRT7 abrogated the effects mediated by miR (show MLXIP Proteins)-519d overexpression in hypertrophic scar fibroblasts.
SIRT7-catalysed histone H3 (show HIST3H3 Proteins) lysine122 desuccinylation is critically implemented in DNA-damage response and cell survival.
Knockdown of SIRT7 leads to the same phenotype as depletion of DDX21 (show DDX21 Proteins) (i.e., increased formation of R loops and DNA double-strand breaks), indicating that SIRT7 and DDX21 (show DDX21 Proteins) cooperate to prevent R-loop accumulation, thus safeguarding genome integrity.
miR (show MLXIP Proteins)-3666 is an important regulator of breast cancer development. The overexpression of miR (show MLXIP Proteins)-3666 inhibits breast cancer cell proliferation by inhibiting SIRT7.
Authors evaluated the expression of known targets of miR (show MLXIP Proteins)-125a and found that sirtuin-7, matrix metalloproteinase-11 (show MMP11 Proteins), and c-Raf (show RAF1 Proteins) were up-regulated in tumor tissue by 2.2-, 3-, and 1.7-fold, respectively. Overall, these data support a tumor suppressor role for miR (show MLXIP Proteins)-125a.
We found a negative correlation between mRNA levels of SIRT1 (show SIRT1 Proteins) in VAT of obese individuals and SIRT7 in VAT of the normal-weight subjects and expression of the relevant miRNAs.
Data indicate the role of SIRT7 in inhibiting SMAD4 (show SMAD4 Proteins)-mediated breast cancer metastasis providing a possible therapeutic avenue.
Energy stress strengthens SIRT7-mediated effects on Akt (show AKT1 Proteins) dephosphorylation.
Data indicate that Sirt7 has a slight protective impact on both the adaptive immune system and neurogenesis. However, overall this epigenetic factor is not capable of impacting the acute or chronic phase of neuroinflammation.
Loss of SIRT7 is associated with Impairment of Adipogenesis and increased Sirt1 (show SIRT1 Proteins) Activity.
the results of our study suggest that SIRT7 is involved in protecting neurons against OGD (show FGFR1 Proteins)/R-induced injury, possibly through regulation of the p53 (show TP53 Proteins)-mediated proapoptotic signaling pathway, indicating a potential therapeutic target for cerebral ischemia/reperfusion injury.
Histological analysis revealed that there is no apparent structural abnormality of the amygdala and hippocampus, which are regions involved in fear memory consolidation, in Sirt7 KO mice. Our results indicate that SIRT7 is involved in the consolidation of fear memory.
Data suggest that high-fat diet (HFD) alters regulation of expression of sirtuins (Sirt4 (show SIRT4 Proteins) and Sirt7) and enzymes in NAD biosynthetic pathway (Tdo2 (show TDO2 Proteins) and Nnmt (show NNMT Proteins)); these alterations are more prominent in liver as compared to white adipose tissue or skeletal muscle; Tdo2 (show TDO2 Proteins) and Nnmt (show NNMT Proteins) may serve as markers of HFD consumption. (Tdo2 (show TDO2 Proteins) = tryptophan 2,3-dioxygenase (show TDO2 Proteins); Nnmt (show NNMT Proteins) = nicotinamide N-methyltransferase (show NNMT Proteins))
The Sirt7 mediates heterochromatin formation at rRNA genes through recruitment of DNA methyltransferase 1 (show DNMT1 Proteins) and another member of the sirtuin (show SIRT1 Proteins) family, Sirt1 (show SIRT1 Proteins).
the decline in SIRT7 in lung fibroblasts has a profibrotic effect, which is mediated by changes in Smad3 (show SMAD3 Proteins) levels.
SIRT7 inhibits TR4 degradation by deacetylation of DDB1.
These results reveal a direct role for SIRT7 in double-strand break repair and establish a functional link between SIRT7-mediated histone H3 (show HIST3H3 Proteins) K18 (show KRT18 Proteins) deacetylation and the maintenance of genome integrity.
miR (show MLXIP Proteins)-93 inhibits the metabolic target Sirt7, which we identified as a major driver of in vivo adipogenesis via induction of differentiation and maturation of early adipocyte precursors.
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined\; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class IV of the sirtuin family.
sirtuin (silent mating type information regulation 2 homolog) 7 (S. cerevisiae)
, sirtuin 7
, novel protein similar to vertebratesirtuin (silent mating type information regulation 2 homolog) 7 (S. cerevisiae) (SIRT7)
, NAD-dependent deacetylase sirtuin-7
, NAD-dependent protein deacetylase sirtuin-7
, SIR2-like protein 7
, regulatory protein SIR2 homolog 7
, silent mating type information regulation 2, S.cerevisiae, homolog 7
, sir2-related protein type 7
, sirtuin type 7
, NAD-dependent deacetylase sirtuin 7