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S5322

Sigma-Aldrich

Anti-Sirt1 (C-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-S. cerevisiae, HOMOLOG-LIKE 1, Anti-SIR2, Anti-SIR2α, Anti-SIR2L1, Anti-Sirtuin 1

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About This Item

MDL number:
MFCD08705602
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~120 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): 5-10 μg using extracts of Jurkat cells
indirect immunofluorescence: 10-20 μg/mL using human U-2-OS cells
western blot: 1-2 μg/mL using whole extracts of Jurkat cells

UniProt accession no.

Q96EB6

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SIRT1(23411)
mouse ... Sirt1(93759)
rat ... Sirt1(309757)

General description

SIRT1 (sirtuin 1) belongs to the silent information regulator (SIR) 2 family and is a class to HDAC (histone deacetylase). It is expressed in various tissues including brain, liver, pancreas, adipose tissue, and skeletal muscle. SIRT1 is also known as the longevity gene.
Sirtuin-1 (SIRT1) resides in the nucleus.

Immunogen

synthetic peptide corresponding to amino acids 723-736 of human SIRT1, conjugated to KLH via an N-terminal cysteine residue.

Application

Anti-Sirt1 (C-terminal) antibody has been used in
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence
  • immunohistochemistry
  • western blotting

Biochem/physiol Actions

SIRT1 (sirtuin 1) functions as a regulator of various metabolic pathways, and influences the pathophysiology of several metabolic diseases. It is a regulator of protein deacetylation, and is a candidate therapeutic target in non-alcoholic fatty liver disease (NAFLD), amyotrophic lateral sclerosis (ALS), kidney disease, and pulmonary disease. It also participates in tumorigenesis, and whether it functions as an oncogene or as a tumor suppressor depends upon the tumor type. In ancreatic ductal adenocarcinoma (PDAC) its elevated expression is linked with poor prognosis, and innon-small-cell lung cancer (NSCLC) it suppresses the expression of tumor suppressor p27. It is also thought to function as a suppressor of cardiovascular disorders, such as myocardial infarction, or neurodegenerative diseases, such as Alzheimer′s disease (AD) or Parkinson′s disorder (PD).
Sirtuin-1 (SIRT1) is a NAD-dependent deacetylase which has been implicated in the regulation of several transcription factors, including p53, forkhead box protein O (FOXO), nuclear factor kappa-B (NFκB), myocyte-specific enhancer factor 2 (Mef2), and peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α).

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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Mammalian SIRT1 represses forkhead transcription factors
Motta M C, et al.
Cell, 116(4), 551-563 (2004)
Nutrient control of glucose homeostasis through a complex of PGC-1 alpha and SIRT1
Rodgers J T, et al.
Nature, 434(7029), 113-113 (2005)
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet A, et al.
Science, 303(5666), 2011-2015 (2004)
Autumn J Broady et al.
Placenta, 50, 44-52 (2017-02-06)
Visfatin/nicotinamide phosphoribosyltransferase (Nampt), an enzyme involved in energy metabolism and sirtuins, SIRT1 and SIRT3, which are NAD-dependent deacetylases, are critical for cellular function. All three either regulate or are regulated by intracellular NAD+ levels and therefore available cellular energy, important for
Inhibition of the NAD-dependent protein deacetylase SIRT2 induces granulocytic differentiation in human leukemia cells
Sunami Y, et al.
PLoS ONE, 8(2), e57633-e57633 (2013)
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