Recombinant Human SIRT6 Protein

Name: Recombinant Human SIRT6 Protein
Brand: Beta LifeScience
SKU: BL-1019SG
Availability: InStock

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Product Overview

Tag	His
Host Species	Human
Accession	NM_016539
Synonym	SIR2L6, Sirtuin 6
Background	SIRT6 is a member of the sirtuin family of proteins which are homologs to the yeast Sir2 protein. Sirtuin family contain a sirtuin core domain and are grouped into four classes with SIRT6 being a member of class IV. Human SIRT6 protein is a NAD(+)-dependent histone H3 lysine-9 deacetylase that modulates telomeric chromatin (1). SIRT6 associates specifically with telomeres and SIRT6 depletion leads to telomere dysfunction with end-to-end chromosomal fusions and premature cellular senescence. SIRT6 -/- mouse cells show that SIRT6 promotes resistance to DNA damage and suppresses genomic instability in association with a role in base excision repair (2).
Description	Recombinant human SIRT6 (23-end) was produced by baculovirus in Sf9 insect cells, fused with a His tag at N-terminus.
Source	Sf9 insect cells
AA Sequence	23a.a.-end
Molecular Weight	~39 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human SIRT6 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	NAD-dependent protein deacetylase involved in various processes including telomere maintenance and gene expression, and consequently has roles in genomic stability, cell senescence and apoptosis. Has very weak deacetylase activity and can bind NAD(+) in the absence of acetylated substrate. Has deacetylase activity towards histone H3K9Ac and H3K56Ac. Modulates acetylation of histone H3 in telomeric chromatin during the S-phase of the cell cycle. May also be required for the association of WRN with telomeres during S-phase and for normal telomere maintenance. Deacetylates histone H3K9Ac at NF-kappa-B target promoters and may down-regulate the expression of a subset of NF-kappa-B target genes. Deacetylation of nucleosomes interferes with RELA binding to target DNA. Acts as a corepressor of the transcription factor Hif1a to control the expression of multiple glycolytic genes to regulate glucose homeostasis. Required for normal IGF1 serum levels and normal glucose homeostasis. Regulates the production of TNF protein. Has a role in the regulation of life span.
Subcellular Location	Nucleus, nucleoplasm. Note=Predominantly nuclear. Associated with telomeric heterochromatin regions.
Protein Families	Sirtuin family, Class IV subfamily
Database References	HGNC: 14934 OMIM: 606211 KEGG: hsa:51548 STRING: 9606.ENSP00000337332 UniGene: Hs.423756

Gene Functions References

experiments revealed the mechanism for SIRT6 in facilitating tumorigenesis and metastasis of colon cancer cells, suggesting that SIRT6 might be a potential therapeutic target for treating colon cancer. PMID: 29227545
SIRT6 inhibited proliferation, migration, and invasion of colon cancer cells by up-regulating PTEN expression and down-regulating AKT1 expression. PMID: 29957460
SIRT6 may suppress cell proliferation, migration, and invasion via inhibition of the NOTCH3 signaling pathway in glioma PMID: 29659670
Downregulation of SIRT6 expression may promote non-small cell lung cancer malignancy in the Chinese Han population. PMID: 29363378
We provide a comprehensive overview of recent developments on the molecular signaling pathways controlled by SIRT1 and SIRT6, two post-translational modifiers proven to be valuable tools to dampen inflammation and oxidative stress at the cardiovascular level PMID: 28661724
Low SIRT6 expression is associated with glioma. PMID: 28677777
Low SIRT6 expression is associated with gastric cancer. PMID: 28656307
miR378b represses the mRNA expression levels of COL1A1 via interference with SIRT6 in human dermal fibroblasts. PMID: 28983623
SIRT6 is a key factor in human development and identifying the first mutation in a chromatin factor behind a human syndrome of perinatal lethality. PMID: 29555651
SIRT6 interacts with and promotes phospho-ATF2 binding to the PGC-1alpha gene promoter to activate its expression. The present study reveals a critical role for SIRT6 in regulating thermogenesis of fat. PMID: 28723567
nf-kappab was was increases duto to SIRT6 silencing in the absence of UV-B PMID: 29465379
p53-dependent SIRT6 expression protects cells from Abeta42-induced DNA damage. PMID: 27156849
Strong correlation has been proved between the expression levels of HDAC4 and SIRT6. PMID: 27766571
SirT6 promotes cysteine ubiquitination in the PRE-SET domain of Suv39h1. PMID: 29317652
this study not only suggests potential roles of SIRT6 in regulating apoptosis and stress resistance via direct deacetylation of p53, but also provides lead compound for the development of potent and selective SIRT6 inhibitors. PMID: 29233643
in vitro and in vivo studies showed that gene silencing of SIRT6 suppressed cell proliferation and promoted cellular apoptosis by activating the Bax-dependent apoptotic signal pathway in Hepatocellular Carcinoma cells. Furthermore, SIRT6 knockdown could increase liver cancer cell sensitivity to chemotherapy drug doxorubicin. SIRT6 is an important protumorigenic factor in liver carcinogenesis. PMID: 26861461
SIRT6 is upregulated in non-small cell lung cancer; it may have a functional role in promoting migration and invasion through ERK1/2/MMP9 signaling PMID: 27777384
Sirt6 inhibits Notch1 and Notch4 transcription by deacetylating histone H3K9. PMID: 28871079
Study shows that SIRT6 protein levels are lower in patients with prediabetes (PreDM) and type 2 diabetes mellitus (T2DM) and implies that SIRT6 may take play in development T2DM by altering the expression of genes involved in glucose metabolism through histone modification rather than its role in DNA repair. PMID: 29197589
Low SIRT6 expression is associated with bone marrow metastasis in neuroblastoma. PMID: 28921546
SIRT6 overexpression suppresses PI3K signaling. PMID: 28228253
post-translational modification facilitates the mobilization of SIRT6 to DNA damage sites and is required for efficient recruitment of poly (ADP-ribose) polymerase 1 (PARP1) to DNA break sites and for efficient repair of double-strand break. PMID: 27568560
SIRT6 and its downstream signaling could be targeted in Alzheimer's disease and age-related neurodegeneration. PMID: 28355558
Loss- and gain-of-SIRT6 function studies in cultured human endothelial cells (ECs) showed that SIRT6 attenuated monocyte adhesion to ECs. PMID: 27249230
The expression of SIRT6 was reduced during cellular senescence, whereas enforced SIRT6 expression promoted cell proliferation and antagonized cellular senescence.Furthermore, SIRT6 directly interacted with p27. Finally, SIRT6 markedly rescued senescence induced by p27. PMID: 27794562
Previously unknown reciprocal influence of SIRT6 and HK2 in regulating autophagy driven monocyte differentiation. PMID: 28935467
our findings describe TRF2 as a novel SIRT6 substrate and demonstrate that acetylation of TRF2 plays a crucial role in the regulation of TRF2 protein stability, thus providing a new route for modulating its expression level during oncogenesis and damage response. PMID: 27923994
SIRT6 over-expression establishes a condition whereby reconfiguration of the Hexokinase 2 promoter chromatin structure makes it receptive to interaction with MZF1/SIRT6 complex, thereby favouring a regulatory state conducive to diminished transcription PMID: 28478957
This study demonstrates that CSNK2A1 and SIRT6 are indicators of poor prognosis for breast carcinomas and that CSNK2A1-mediated phosphorylation of SIRT6 might be involved in the progression of breast carcinoma. PMID: 27746184
Thus, these results reveal that SUMOylation has an important role in regulation of Sirt6 deacetylation on H3K56, as well as its tumor suppressive activity. PMID: 26898756
HBx increased signs of DNA damage such as accumulation of 8-hydroxy-2'-deoxyguanosine and comet formation, which were reversed by overexpression of PARP1 and/or Sirt6..physical interaction of HBx and PARP1 accelerates DNA damage by inhibiting recruitment of the DNA repair complex to the damaged DNA sites, which may lead to the onset of hepatocarcinogenesis PMID: 27041572
Data suggest, in macrophages, SIRT6 plays role in preventing atherosclerosis by reducing foam cell formation via autophagy-dependent pathway involving regulation of expression of ATG5, LC3B, LAMP1, ABCA1, ABCG1, and MIRN33. (ATG5 = autophagy-related protein 5; LC3B = microtubule-associated protein 1 light chain 3 beta; LAMP1 = lysosomal-associated membrane protein 1; ABCA1/ABCG1 = ATP-binding cassette transporters 1/8) PMID: 28296196
These findings reveal a previously unknown role for nasal mucosa steady-state conditions in the control of Sirt6 activity, and provide evidence for a relationship between HMGB1 and Sirt6 in chronic rhinosinusitis with nasal polyps (CRSwNP), and promising benefits of glycyrrhetinic acid for CRSwNP patients. PMID: 28685526
In obese patients, the expression of Sirt6 expression is reduced. PMID: 28250020
positive regulator of aldose reductase expression in U937 and HeLa cells under osmotic stress PMID: 27536992
these results suggest that SIRT6 enhances cell aggressiveness in PTC via BRAF/ERK/Mcl1 pathway, and thus may be a promising target in the treatment of the disease. PMID: 28393212
our studies shed insights into the crucial functions of sirtuin 6 in esophageal carcinoma cells and provide evidence supporting sirtuin 6-based personalized therapies in esophageal carcinoma cell patients PMID: 28653878
acts as a tumor promoter by preventing DNA damage and cellular senescence in hepatocellular carcinoma PMID: 27824900
SIRT6 promotes deacetylation of a new substrate, residue K18 of histone H3 (H3K18), and inactivation of SIRT6 in cells leads to H3K18 hyperacetylation and aberrant accumulation of pericentric transcripts. PMID: 27043296
Data show that the increased acetylation of Ku autoantigen 70kDa (Ku70) in sirtuin 6 protein (SIRT6)-depleted cells disrupt its interaction with Bax apoptosis regulator protein (Bax), which finally resulted in Bax mitochondrial translocalization. PMID: 28238784
Taken together, these data demonstrated that astragaloside IV sensitized tumor cells to gefitinib via regulation of SIRT6, suggesting that astragaloside IV may serve as potential therapeutic approach for lung cance PMID: 28443459
SIRT6 prevents matrix degradation of nucleus pulposus via the NF-kappaB signaling pathway in intervertebral disc degeneration. SIRT6 physically interacted with nuclear factor-kappaB (NF-kappaB). PMID: 28215636
The single nucleotide polymorphisms rs117385980 (C;T) in sirtuin 6 , situated 23 bases downstream of the exon 2 exon/intron border was found in heterozygous form in 1/43 longer-living healthy men (Minor allele frequency (MAF) 0,0116) and in 9/92 controls. PMID: 28399814
In the model of CIA, forced expression of SIRT6 ameliorated disease progression, osteoblastic synthesis of Cyr61, and macrophage recruitment. More importantly, expression of LDHA and oxidative lesions were decreased in osteoblasts of SIRT6-treated joints. Our findings suggest that SIRT6 suppresses inflammatory response in osteoblasts via modulation of glucose metabolism and redox homeostasis. PMID: 27534902
The data indicate that distinct activities of SIRT6 regulate different pathways and that the G60A mutant is a useful tool to study the contribution of defatty-acylase activity to SIRT6's various functions. PMID: 27322069
this study shoes that through the antiglycolytic activity of SIRT6, the autophagy is suppressed, which is beneficial to nasal polyp formation PMID: 26803106
The promoter regions of the SIRT6 gene were genetically analyzed in large cohorts of MI patients (n = 371) and ethnically-matched controls (n = 383). Results: A total of 15 DNA sequence variants (DSVs) were identified, including seven single-nucleotide polymorphisms (SNPs). Two novel heterozygous DSVs, g.4183823G>C and g.4183742G>A, were identified in two MI patients but in none of the controls. PMID: 26886147
we examined the role and mechanisms of SIRT6 in suppressing postoperative epidural scar formation. We showed that SIRT6 promoted the expression of miR-21 and then suppressed TGF-beta2 expression in a targeted manner. PMID: 26987016
SIRT6 induced autophagy via attenuation of AKT signaling and treatment with autophagy inhibitor 3-MA or knockdown of autophagy-related protein Atg5 rescued H2O2-induced neuronal injury. PMID: 26983852
SIRT6 as an important pancreatic ductal adenocarcinoma tumor suppressor PMID: 27180906

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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