Recombinant Human NAD-dependent protein deacetylase sirtuin-1(SIRT1)

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Code CSB-EP822202HU
Size US$1726
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names SIRT1
Uniprot No. Q96EB6
Research Area Epigenetics and Nuclear Signaling
Alternative Names 75SirT1; hSIR2; hSIRT1; HST2; HST2, S. cerevisiae, homolog of; NAD dependent deacetylase sirtuin 1; NAD dependent protein deacetylase sirtuin 1; NAD-dependent deacetylase sirtuin-1 ; OTTHUMP00000198111; OTTHUMP00000198112; Regulatory protein SIR2 homolog 1; SIR1_HUMAN; SIR2; SIR2 like 1; SIR2 like protein 1; SIR2, S.cerevisiae, homolog-like 1; SIR2-like protein 1; SIR2ALPHA; SIR2L1; Sirt1; SirtT1 75 kDa fragment; Sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae); Sirtuin 1; Sirtuin type 1
Species Homo sapiens (Human)
Source E.coli
Expression Region 2-747aa
Target Protein Sequence ADEAALALQPGGSPSAAGADREAASSPAGEPLRKRPRRDGPGLERSPGEPGGAAPEREVPAAARGCPGAAAAALWREAEAEAAAAGGEQEAQATAAAGEGDNGPGLQGPSREPPLADNLYDEDDDDEGEEEEEAAAAAIGYRDNLLFGDEIITNGFHSCESDEEDRASHASSSDWTPRPRIGPYTFVQQHLMIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELAYLSELPPTPLHVSEDSSSPERTSPPDSSVIVTLLDQAAKSNDDLDVSESKGCMEEKPQEVQTSRNVESIAEQMENPDLKNVGSSTGEKNERTSVAGTVRKCWPNRVAKEQISRRLDGNQYLFLPPNRYIFHGAEVYSDSEDDVLSSSSCGSNSDSGTCQSPSLEEPMEDESEIEEFYNGLEDEPDVPERAGGAGFGTDGDDQEAINEAISVKQEVTDMNYPSNKS
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 85.5kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Basically, we can dispatch the products out in 3-7 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

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 Q&A
Q:

An M is missing in the beginning of the sequence. Why the M is missing in the beginning. Any particular reason?

A:
Thanks for your inquiry. The M at begining is the initiation codon, and in the organism self-expression, it will be cutted. So when we choose the express region, we didn't choose it.

Target Data

Function NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell
Gene References into Functions
  1. These results suggest that resveratrol induces chondrosarcoma cell apoptosis via a SIRT1-activated NF-kappaB (p65 subunit of NF-kappaB complex)deacetylation and exhibits anti-chondrosarcoma activity in vivo. PMID: 28600541
  2. I157172 induced upregulation of SIRT1, and downregulation of acetyl-STAT3. PMID: 30365149
  3. SIRT1-mediated H3K9 deacetylation helps to maintain gene repression but is not required for the direct ZEB2 repressive function.SIRT1 activity maintains the stability of ZEB2-induced RAB25 repression. PMID: 30445998
  4. Data show that long non-coding RNA MALAT1 (MALAT1) repressed sirtuin 1 (SIRT1) expression through targeting forkhead box protein O1 (Foxo1). PMID: 29928873
  5. SIRT1 had a pivotally protective role in the regulation of ADSCs aging and apoptosis induced by H2O2 PMID: 29803744
  6. plasma levels correlated inversely with all studied adiposity and atherogenicity indices in metabolic syndrome patients with and without prediabetes PMID: 29779969
  7. Increased SIRT1 activity protects against diabetes-induced podocyte injury and effectively mitigates the progression of diabetic kidney disease. PMID: 29477240
  8. the Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins PMID: 28504272
  9. Adipose tissue sirtuin 1 was related to insulin sensitivity. The relationship was still present after controlling for BMI, however, it disappeared after controlling for adipose tissue SLC2A4. Muscle sirtuin 1 was not related to insulin sensitivity. PMID: 29417372
  10. data suggest that SIRT1 is an oncogenic factor in breast cancer cells and can be involved in the progression of breast cancer by inhibiting p53 and activating POLD1 PMID: 29807012
  11. SIRT1 expression is significantly upregulated in paclitaxel-resistant cervical cancer tissues and cell lines compared to normal tissues or PTX-sensitive CC tissues and cell lines. Knockdown of SIRT1 inhibited the cell proliferation, promoted cell cycle arrest and apoptosis of PTX-sensitive CC cells, and decreased the expression of MDR proteins. PMID: 29808798
  12. In our retrospective study, high SIRT1 expression significantly correlated with vascular invasion and a worse prognosis in colorectal cancer PMID: 30082156
  13. SIRT1 polymorphisms and their expression were associated with the presence of alcoholic fatty liver disease (AFLD), and there was a close relationship among four SNPs and body mass index in AFLD patients, but no SNP was related to its expression. PMID: 29189974
  14. The variable role of SIRT1 in the maintenance and differentiation of mesenchymal stem cells. PMID: 29715067
  15. Results indicate that SIRT1 may promote the metastasis of chondrosarcoma by inducing epithelial-mesenchymal transition and can be a potential molecular target for chondrosarcoma therapy. PMID: 28112277
  16. Regulation of transmembrane-4-L-six-family-1 (TM4SF1) on bladder cancer cell could be induced by peroxisome proliferator-activated receptor gamma (PPARgamma)-sirtuin 1 (SIRT1) feedback loop. PMID: 29175458
  17. Results present evidence that SIRT1 plays an essential role in regulating the transcription of CLDN5 likely by modifying and modulating the activity of KLF4 in ovarian cancer cells. PMID: 28888043
  18. results suggest that seminal SIRT1 expression has a role in male infertility PMID: 29359516
  19. SIRT1 may promote the transformation of tumor cells by inducing the epithelial-mesenchymal transition. PMID: 29656187
  20. relevance of the discovered Sirt1-Smad2 interaction for the regulation of TGFbeta-dependent gene transcription PMID: 29187201
  21. Bioinformatics and the dual luciferase reporter assay analysis results demonstrated that miR-29a specifically targeted the 3'-UTR of SIRT1 mRNA and regulated its protein expression. Increased SIRT1 expression rescued the inhibited effects induced by miR-29a overexpression in HCC cells. PMID: 29630527
  22. High Sirt1 Expression is associated with Gastric cancer. PMID: 29693338
  23. Sirt1 protects against oxidative stress-induced apoptosis in fibroblasts from psoriatic patients. PMID: 29799444
  24. Investigated the effect of statins on the expression of sirtuin 1 (SIRT1) and endothelial nitric oxide synthase 3 (eNOS) proteins in young premature myocardial infarction (PMI) patients. Found patients with PMI who were taking statins had a markedly higher level of SIRT1 compared with the controls. The level of eNOS protein was considerably lower in PMI patients compared with the control group. PMID: 29664427
  25. Clinical data are the first to identify SIRT1 as an important regulator of hepatocellular function in human liver transplants under ischemia/reperfusion stress. PMID: 28719070
  26. suggests SIRT1 may serve as a predictor of poor prognosis in esophageal squamous cell carcinoma, and its mediated tumor-promoting role might be associated with the overexpression of EGFR protein in esophageal squamous cell carcinoma PMID: 29625788
  27. findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan PMID: 29133780
  28. This study represents the important role of Sirt1 and senescence in the regulation of beige adipocyte differentiation during aging. PMID: 29678576
  29. Baicalin activated the SIRT1/AMPK and mechanistic target of rapamycin (mTOR), and SIRT1/AMPK and matrix metalloproteinase (MMP) signaling in A549 and H1299 cells in a dose-dependent manner. siRNA silencing of SIRT1 and AMPK reduced the effects of baicalin on cell proliferation and migration. PMID: 29632297
  30. 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 levell PMID: 28661724
  31. SIRT1 was identified as a direct target of miR-212 and its expression was inversely correlated with miR-212 expression in thyroid cancer tissues. Overexpression of SIRT1 could effectively rescue miR-212 mimic-induced suppression of cell proliferation, migration and invasion in TPC-1 thyroid cancer cell line. PMID: 29207181
  32. The present study is the first to report a significant association between SIRT1 polymorphisms and antisocial personality in adolescents. PMID: 28439078
  33. Studied effects of dexamethasone on gene expression regulation of sirtuin 1 (SIRT1), interleukin 6 (IL6), and endothelin 1 (EDN1) in gingival derived aging stem cells. Dexamethasone downregulated expression of SIRT1 and IL6 but upregulated EDN1 in stem cells. PMID: 29302812
  34. miR-200a and its target gene, SIRT1, may exert a possible role in induction of apoptosis in dopaminergic neurons. PMID: 29936262
  35. The rhuschalcone I analogue (9) showed the best activity against sirt1, with an IC50 value of 40.8 microM. Based on the docking experiments, suggestions for improving the biological activities of the newly identified hit compounds have been provided. PMID: 29443909
  36. Results indicated that SIRT1 contributes to the neuroprotection of salidroside against MPP(+) -induced apoptosis and oxidative stress, in part through suppressing of mitogen-activated protein kinase (MAPK) pathways. PMID: 28851138
  37. decreased SIRT1 expression and its SUMOylation by SUMO1 and SUMO2/3 may be associated with the development of bronchopulmonary dysplasia. PMID: 29115559
  38. The nicotinamide adenine dinucleotide (NAD)-dependent deacetylase SIRT1 acts as an energy sensor and negatively regulates poly(A)RNA transport via deacetylating a poly(A)-binding protein, PABP1. PMID: 28756945
  39. L-Carnitine alleviated epithelial mesenchymal transformation-associated renal fibrosis caused by perfluorooctanesulfonate through a Sirt1- and PPARgamma-dependent mechanism. PMID: 28973641
  40. High SIRT1 expression is associated with hepatocellular carcinoma. PMID: 28677784
  41. No significant association has been discovered between SIRT1 polymorphisms and diabetic foot severity or characteristics PMID: 29995800
  42. A significant correlation between the physical activity level and peripheral blood mononuclear cell SIRT1 and FOXO1 mRNA expression was found in COPD patients. PMID: 29138552
  43. Defective sirtuin-1 was found to increase IL-4 expression through acetylation of GATA-3 in patients with severe asthma compared with healthy controls. PMID: 26627546
  44. SIRT1 gene polymorphisms can have direct and indirect effects on the pathogenesis of coronary artery diseases. PMID: 29885463
  45. miR-146 exerted protective functions might be via up-regulation of Sirt1 thereby blocking NF-kappaB and Notch pathways. PMID: 29229881
  46. results suggested that SIRT1 deficiency in Bladder cancer cells could suppress cell viability by activating antioxidant response and inducing cell cycle arrest possibly via FOXO3a-related pathways. PMID: 29147649
  47. These observations provide further evidence for a critical tumor-suppressive role of the miR-200a in renal cell carcinoma (RCC) in addition to identifying a novel regulatory mechanism, which may contribute to SIRT1 upregulation in RCC. PMID: 28717923
  48. Results showed that RSV or overexpression of SIRT1 elicited inhibitory effects on NMDA-induced excitotoxicity including a decrease in cell viability, an increase in lactate dehydrogenase (LDH) release, and a decrease in the number of living cells as measured by CCK-8 assay, LDH test, and Calcein-AM and PI double staining. PMID: 29081884
  49. results indicate that FOXO1 inhibits gastric cancer (GC) growth and angiogenesis under hypoxic conditions via inactivation of the HIF-1alpha-VEGF pathway, possibly in association with SIRT1; thus, development of treatment modalities aiming at this pathway might be useful for treating GC PMID: 25761483
  50. Data suggest the activity restoration role of resveratrol toward some "loose-binding" substrates of sirtuin 1 (SIRT1), and has implications for the rational design of new substrate-specific SIRT1 modulators. PMID: 27901083

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Subcellular Location Nucleus, PML body, Cytoplasm, Nucleus
Protein Families Sirtuin family, Class I subfamily
Tissue Specificity Widely expressed.
Database Links

HGNC: 14929

OMIM: 604479

KEGG: hsa:23411

STRING: 9606.ENSP00000212015

UniGene: Hs.369779

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