추천 제품
생물학적 소스
rabbit
Quality Level
결합
unconjugated
항체 형태
affinity isolated antibody
항체 생산 유형
primary antibodies
클론
polyclonal
양식
buffered aqueous solution
분자량
antigen ~120 kDa
종 반응성
human
농도
~1.0 mg/mL
기술
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 수납 번호
배송 상태
dry ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... SIRT1(23411)
mouse ... Sirt1(93759)
rat ... Sirt1(309757)
일반 설명
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.
면역원
synthetic peptide corresponding to amino acids 723-736 of human SIRT1, conjugated to KLH via an N-terminal cysteine residue.
애플리케이션
Anti-Sirt1 (C-terminal) antibody has been used in
- immunoblotting
- immunoprecipitation
- immunofluorescence
- immunohistochemistry
- western blotting
생화학적/생리학적 작용
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).
물리적 형태
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
면책조항
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 Code
10 - Combustible liquids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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
Mammalian SIRT1 represses forkhead transcription factors
Motta M C, et al.
Cell, 116(4), 551-563 (2004)
SIRT1 is a novel regulator of key pathways of human labor
Lappas M, et al.
Biology of Reproduction, 84(1), 167-178 (2011)
Pai-Jong Stacy Tsai et al.
Reproductive sciences (Thousand Oaks, Calif.), 22(8), 1028-1036 (2015-02-12)
Visfatin is both a systemic adipocytokine and the cytosolic enzyme, nicotinamide phosphoribosyl transferase (Nampt). This is a longevity protein, which extends the lifespan of human cells by activating sirtuin 1 (SIRT1). In this study, we sought a role for these
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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