产品名称
Anti-Sirt1 (C-terminal) 兔抗, ~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
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.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... SIRT1(23411)
mouse ... Sirt1(93759)
rat ... Sirt1(309757)
Physical form
0.01M 磷酸缓冲盐溶液,pH 7.4,含 15mM 叠氮化钠。
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).
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.
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.
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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
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)
Mammalian SIRT1 represses forkhead transcription factors
Motta M C, et al.
Cell, 116(4), 551-563 (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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