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MilliporeSigma

S5947

Sigma-Aldrich

Anti-Sirt7 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-SIR2L7, Anti-Sir2-related protein type 7, Anti-Sirtuin (silent mating type information regulation 2 homolog) 7

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~45 kDa

species reactivity

mouse (predicted), human

technique(s)

immunoprecipitation (IP): 2-4 μg using extracts of HEK-293T cells expressing human Sirt7
indirect immunofluorescence: 2-4 μg/mL using human HEK-293T cells
western blot: 1-2 μg/mL using whole extracts of HEK-293T cells expressing human Sirt7

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SIRT7(51547)
mouse ... Sirt7(209011)

General description

Nicotinamide adenine dinucleotide (NAD)-dependent histone deacetylase (Sir2) is one of the silent information regulator genes in yeast. It belongs to a family of proteins, that is found in organisms ranging from bacteria to complex eukaryotes. Proteins of this family share a core domain showing 25-60% sequence identity. The mammalian Sir2 gene family is comprised of seven members which are designated as Sirt1-7.

Immunogen

synthetic peptide corresponding to amino acids 35-51 of human Sirt7, conjugated to KLH via a C-terminal cysteine residue. The sequence is identical in mouse.

Application

Anti-Sirt7 antibody produced in rabbit has been used in western blotting analysis and immunofluorescence detection.

Biochem/physiol Actions

Sirt7 (sirtuin 7) is extensively found in protein associated with active rRNA genes (rDNA), in the nucleolus. It interacts with RNA polymerase I (Pol I) and histones. Overexpression of Sirt7 increases Pol I-mediated transcription, whereas knockdown of Sirt7 or inhibition of its catalytic activity results in decreased association of Pol I with rDNA and reduces Pol I transcription. Depletion of Sirt7 stops cell proliferation and triggers apoptosis. High levels of Sirt7 expression are associated with breast cancer.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability.
Brachmann CB, et al.
Genes & Development, 9(23), 2888-2902 (1995)
Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis
Grob A, et al.
Journal of Cell Science, 122(4), 489-498 (2009)
Altered sirtuin expression is associated with node-positive breast cancer
Ashraf N, et al.
British Journal of Cancer, 95(8), 1056-1056 (2006)
Shashi Kiran et al.
The FEBS journal, 280(14), 3451-3466 (2013-05-18)
Sirtuins belong to a class of NAD-dependent deacetylases, and include seven distinct isoforms, of which SIRT7 is the least studied member. In the present study, the subcellular expression of SIRT7 in primary fibroblasts undergoing senescence was evaluated by immunocytochemistry and
The human silent information regulator (Sir) 2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
Schwer B, et al.
The Journal of Cell Biology, 158(4), 647-657 (2002)

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