Recombinant Human Nad-Dependent Protein Deacetylase Sirtuin-7 (SIRT7) Protein (His&Myc)

Name: Recombinant Human Nad-Dependent Protein Deacetylase Sirtuin-7 (SIRT7) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06706P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Nad-Dependent Protein Deacetylase Sirtuin-7 (SIRT7) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9NRC8
Target Symbol	SIRT7
Synonyms	(NAD-dependent protein deacylase sirtuin-7)Regulatory protein SIR2 homolog 7)(SIR2-like protein 7)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MAAGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESADLVTELQGRSRRREGLKRRQEEVCDDPEELRGKVRELASAVRNAKYLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRSVSAADLSEAEPTLTHMSITRLHEQKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCVPNREYVRVFDVTERTALHRHQTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASRADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVMRLLMAELGLEIPAYSRWQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT
Expression Range	1-400aa
Protein Length	Full Length
Mol. Weight	52.3 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase and deglutarylase), depending on the context. Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes. Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53. Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex. Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region. In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription. Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis. Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex. Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65. Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation. Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II. Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL. Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1. Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51. Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases. In addition to protein deacetylase activity, also acts as protein-lysine deacylase. Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts. Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes. Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair. Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation. Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina. Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability. Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity.
Subcellular Location	Nucleus, nucleolus. Nucleus, nucleoplasm. Chromosome. Cytoplasm.
Protein Families	Sirtuin family, Class IV subfamily
Database References	HGNC: 14935 OMIM: 606212 KEGG: hsa:51547 STRING: 9606.ENSP00000329466 UniGene: Hs.514636

Gene Functions References

Our study provides evidence that the miR-340/SIRT7 axis may play an important role in the molecular pathogenesis of angiosarcoma. PMID: 29710664
Our data confirmed that SIRT7 was overexpressed in cholangiocarcinoma patient tissues and cell lines. PMID: 29438839
SIRT7 is involved in regulating TGF-beta1-induced ASM cell proliferation. PMID: 29843083
Overexpression of SIRT7 abrogated the effects mediated by miR-519d overexpression in hypertrophic scar fibroblasts. PMID: 29428666
SIRT7-catalysed histone H3 lysine122 desuccinylation is critically implemented in DNA-damage response and cell survival. PMID: 27436229
Knockdown of SIRT7 leads to the same phenotype as depletion of DDX21 (i.e., increased formation of R loops and DNA double-strand breaks), indicating that SIRT7 and DDX21 cooperate to prevent R-loop accumulation, thus safeguarding genome integrity. PMID: 28790157
miR-3666 is an important regulator of breast cancer development. The overexpression of miR-3666 inhibits breast cancer cell proliferation by inhibiting SIRT7. PMID: 28944911
Authors evaluated the expression of known targets of miR-125a and found that sirtuin-7, matrix metalloproteinase-11, and c-Raf 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-125a. PMID: 28445974
Data indicate the role of SIRT7 in inhibiting SMAD4-mediated breast cancer metastasis providing a possible therapeutic avenue. PMID: 28827661
Energy stress strengthens SIRT7-mediated effects on Akt dephosphorylation. PMID: 28147277
The SIRT7 is mobilized from the nucleolus to the nucleoplasm and promotes DDB1 deacetylation, leading to decreased DDB1-CUL4 association and CRL4 activity. PMID: 28886238
Data suggest that SIRT7 undergoes Lys-63 polyubiquitination, later removed by USP7 to repress enzymatic activity of SIRT7; USP7 and SIRT7 regulate gluconeogenesis via expression of glucose-6-phosphatase catalytic subunit (G6PC); SIRT7 targets G6PC promoter through ELK4. (SIRT7 = sirtuin 7; USP7 = ubiquitin specific peptidase 7; G6PC = glucose-6-phosphatase catalytic subunit; ELK4 = transcription factor ELK4) PMID: 28655758
the decline in SIRT7 in lung fibroblasts has a profibrotic effect, which is mediated by changes in Smad3 levels. PMID: 28385812
SIRT7 inhibits TR4 degradation by deacetylation of DDB1. PMID: 28623141
miR-152/SIRT7 axis plays a key role in the regulation of Human dental pulp stem cell senescence. PMID: 26991832
our study suggests that SIRT7 functions as an oncogene in non-small cell lung cancer (NSCLC), and miR-3666 can target SIRT7 to inhibit NSCLC cell growth by promoting the pro-apoptotic signaling pathway PMID: 27599551
SIRT7 trans-represses RPS7 gene in the presence of HBx protein.HBx enhances intracellular stability of SIRT7 protein. PMID: 26442981
This study showed that SIRT7 can be activated by DNA to hydrolyze the acetyl group from lysine residues in vitro on histone peptides and histones in the chromatin context. PMID: 26907567
Novel interactions of TPPII, p53, and SIRT7 presented in this study might contribute to the knowledge of the regulatory effects of these proteins on apoptotic pathways and to the understanding mechanisms of aging and lifespan regulation. PMID: 26169984
SIRT7 deacetylates U3-55k, enhancing U3-55k binding to U3 snoRNA, which is a prerequisite for pre-rRNA processing. PMID: 26867678
this is the first report on the regulation mechanism of SIRT7 gene, in which, HDAC3 collaborated with C/EBPalpha to occupy its responding element in the upstream region of SIRT7 gene and repressed its expression in human cells. PMID: 26704017
Sirt7 expression was implicated with high histological grade and independently predicted poor clinical outcome in patients with breast cancer, suggesting that Sirt7 might play a role in the malignant progression of breast cancer. PMID: 25973086
SIRT7 might play a role of oncogene in ovarian malignancy. Down-regulation of SIRT7 significantly reduced ovarian cancer cell growth, repressed colony formation and increased cancer cell apoptosis; up-regulation promoted the migration of cancer cells. PMID: 25921180
Sirt7 is overexpressed in human gastric cancers. Expression of Sirt7 is markedly correlated with tumor size, metastasis, disease stage and prognosis. PMID: 25860861
SIRT7 expression was reduced in aged hematopoietic stem cells (HSCs), and SIRT7 up-regulation improved the regenerative capacity of aged HSCs. PMID: 25792330
Interactions of two highly acetylated proteins, nucleophosmin (NPM1) and nucleolin, with SIRT6 and SIRT7 were confirmed by co-immunoprecipitation. PMID: 24782448
In the cancer group, the expression level of SIRT6 and SIRT7 were significantly up-regulated and are potential circulating prognostic markers for head and neck squamous cell carcinoma. PMID: 25503141
stress-induced Sirt7 inhibition significantly increases stress resistance and modulates insulin/IGF-1 signaling pathways. PMID: 24885964
High Sirtuin 7 promotes cellular survival following genomic stress by attenuation of DNA damage, SAPK activation and p53 response in osteosarcoma. PMID: 25445786
Our findings suggest that Sirt7 plays an important role in the development and progression of human colorectal cancer and functions as a valuable marker of colorectal cancer prognosis. PMID: 24771643
These findings place SIRT7 at the crossroads of chromatin signaling, metabolic, and tumor-regulatory pathways. Thus, SIRT7 is a promising pharmacologic target for epigenetic cancer therapy. PMID: 24536059
Study identifies SIRT7 as a cofactor of Myc for transcriptional repression and delineates a druggable regulatory branch of the ER stress response that prevents and reverts fatty liver disease. PMID: 24210820
We propose that SIRT7 is involved in multiple pathways involved in ribosome biogenesis, and we hypothesize that its down-regulation may contribute to an antitumor effect, partly through the inhibition of protein synthesis. PMID: 24113281
The results identify a nonhistone target of SIRT7 and uncover an RNA-mediated mechanism that adapts nucleolar transcription to stress signaling PMID: 24207024
Knockdown of Sirt7 led to an increase in HIF-1alpha and HIF-2alpha protein levels and an increase in HIF-1 and HIF-2 transcriptional activity. PMID: 23750001
Idenitifcation of the nuclear localization sequence in human SIRT7 and an association between loss of nucleolar SIRT7 and replicative senescence. PMID: 23680022
Our findings suggest the oncogenic potential of SIRT7 in hepatocarcinogenesis. PMID: 23079745
SIRT7 plays a crucial role in connecting the function of chromatin remodeling complexes to RNA Pol I machinery during transcription PMID: 22586326
work establishes SIRT7 as a highly selective H3K18Ac deacetylase and demonstrates a pivotal role for SIRT7 in chromatin regulation, cellular transformation programs and tumour formation in vivo. PMID: 22722849
Fluorescence in situ hybridization analysis localized the Sirt7 gene to chromosome 17q25.3; a region which is frequently affected by chromosomal alterations in acute leukemias and lymphomas. PMID: 16525639
SIRT7 is a positive regulator of Pol I transcription and is required for cell viability in mammals. PMID: 16618798
Levels of SIRT7 expression were significantly increased in breast cancer PMID: 17003781
associated with NORs during mitosis,interacts with the rDNA transcription factor UBF,phosphorylated via the CDK1-cyclin B pathway during mitosis and dephosphorylated by a phosphatase sensitive to okadaic acid at exit from mitosis PMID: 19174463
SIRT7 is required for the resumption of rDNA transcription at the exit from mitosis. PMID: 19174463

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