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Merck

S8447

Sigma-Aldrich

Anti-Sirt2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-SIR2L, Anti-SIR2L2, Anti-Sirtuin (silent mating type information regulation 2 homolog), Anti-sirtuin 2

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About This Item

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

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 37:43 kDa (rat)
antigen 43 kDa (human)

species reactivity

rat, mouse, human

packaging

antibody small pack of 25 μL

technique(s)

immunoprecipitation (IP): 2-5 μg using extract of COS7 cells or 293 cells expressing recombinant human SIRT2 protein.
indirect immunofluorescence: 5-10 μg/mL using human HeLa cells.
western blot: 1-2 μg/mL using whole extracts of mouse and rat brain.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SIRT2(22933)
mouse ... Sirt2(64383)
rat ... Sirt2(361532)

General description

Rabbit polyclonal anti-Sirt2 antibody recognizes mouse, rat (37/43 kDa), and human (43 kDa) Sirt2. Detection of the Sirt2 bands by immunoblotting is specifically inhibited with the immunizing peptide.
Sirt2 is an NAD+-dependent tubulin deacetylase. Two Sirt2 isoforms exist as the result of alternative splicing. Sirt2 is overexpressed during mitosis and is multiply phosphorylated at the G2/M transition of the cell cycle, indicating that it plays a role in the control of mitotic exit in the cell cycle. Although Sirt2 resides predominantly in the cytoplasm, it becomes enriched in the nucleus during the cell cycle where it is associated with mitotic structures. Sirt2 was found to be an oligodendroglial protein that affects cell differentiation through deacetylating α-tubulin.
Sirtuin 2 (SIRT2) is a cytoplasmic protein, which is part of the sirtuin family of proteins. SIRT2 colocalizes with microtubules. This gene is located on human chromosome 19q13.2.

Immunogen

synthetic peptide corresponding to amino acids 341-352 of mouse Sirt2, conjugated to KLH. The corresponding sequence is identical in rat and differs by one amino acid in human Sirt2.

Application

Anti-Sirt2 antibody has been used in western blotting and immunofluorescence.
Rabbit polyclonal anti-Sirt2 antibody may be used in several applications including immunoblotting, immunoprecipitation, and immunofluorescence.

Biochem/physiol Actions

Sirtuin 2 (SIRT2) maintains the integrity of the genome. Inhibition of SIRT2 can lead to neuroprotection in cellular and invertebrate models of Huntington′s disease. SIRT2 can deacetylate lys40 of α-tubulin both in vitro and in vivo. Knockdown of SIRT2 by small interfering RNA (siRNA) leads to tubulin hyperacetylation.

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

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificados de análisis (COA)

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Visite la Librería de documentos

SIRT2 is required for efficient reprogramming of mouse embryonic fibroblasts toward pluripotency
Kim A Y, et al.
Cell Death & Disease, 9(9), 893-893 (2018)
SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis
Luthi-Carter R, et al.
Proceedings of the National Academy of Sciences of the USA, 201002924-201002924 (2010)
Sirtuin 2 mutations in human cancers impair its function in genome maintenance
Head P E, et al.
The Journal of biological chemistry, jbc-M116 (2017)
Differential expression of sirtuin family members in the developing, adult, and aged rat brain
Sidorova-Darmos E, et al.
Frontiers in Aging Neuroscience, 6(3), 333-333 (2014)
SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo
Bobrowska A, et al.
Testing, 7(4), e34805-e34805 (2012)

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