05-1243
Anti-Sirt1 Antibody, clone 3H10.2
clone 3H10.2, Upstate®, from mouse
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关于此项目
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
3H10.2, monoclonal
Application:
immunoprecipitation (IP)
western blot
western blot
Species reactivity:
human
Citations:
18
Technique(s):
immunoprecipitation (IP): suitable
western blot: suitable
western blot: suitable
Uniprot accession no.:
产品名称
Anti-Sirt1 Antibody, clone 3H10.2, clone 3H10.2, Upstate®, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified antibody
antibody product type
primary antibodies
clone
3H10.2, monoclonal
species reactivity
human
manufacturer/tradename
Upstate®
technique(s)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... SIRT1(23411)
Analysis Note
routinely evaluated by immunoblot on nuclear extract from HeLa cells
Application
Anti-Sirt1 Antibody, clone 3H10.2 is a Mouse Monoclonal Antibody for detection of Sirt1 also known as Sirtuin 1, Silent mating type Information Regulation-2 & has been tested in IP & WB.
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Histones
Histones
Biochem/physiol Actions
Human Sirt1. Does not cross react with lysates from mouse NIH/3T3 cells or rat PC12 cells.
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
120 kDa
The Sir2 protein in yeast is known to function in transcriptional silencing processes through the deacetylation of histones H3 and H4. The more recently described human homologue of Sir2, known as SIRT1, has been found to associate with the tumor suppressor protein p53. There are now five described human homologs of yeast Sir2, which are named SIRT1-5.
SIRT1 binds and deacetylates p53 with specificity for its C-terminal Lys382 residue in response to the upregulation of promyelocytic leukemia protein (PML) nuclear bodies or oncogenic Ras. The deacetylation of p53 SIRT1 has been shown to negatively regulate p53-mediated transcription, preventing cellular senescence and apoptosis induced by DNA damage and stress. SIRT1 is a HDAC which is important in establishing repressive chromatin structures and plays a role in increasing lifespan.
SIRT1 binds and deacetylates p53 with specificity for its C-terminal Lys382 residue in response to the upregulation of promyelocytic leukemia protein (PML) nuclear bodies or oncogenic Ras. The deacetylation of p53 SIRT1 has been shown to negatively regulate p53-mediated transcription, preventing cellular senescence and apoptosis induced by DNA damage and stress. SIRT1 is a HDAC which is important in establishing repressive chromatin structures and plays a role in increasing lifespan.
Immunogen
GST fusion protein corresponding to amino acids 508-616 of human Sirt1.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: 05-707
Physical form
Format: Purified
Protein G Purified
Purified in PBS with 0.05% Sodium Azide
Preparation Note
Maintain at 2-8 °C in undiluted aliquots for up to 6 months after date of receipt. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
p53 Activation: a case against Sir.
Brooks, Christopher L and Gu, Wei
Cancer Cell, 13, 377-378 (2008)
Timour Prozorovski et al.
Nature cell biology, 10(4), 385-394 (2008-03-18)
Repair processes that are activated in response to neuronal injury, be it inflammatory, ischaemic, metabolic, traumatic or other cause, are characterized by a failure to replenish neurons and by astrogliosis. The underlying molecular pathways, however, are poorly understood. Here, we
Hsiang-Yu Chang et al.
Nature communications, 4, 2757-2757 (2013-11-14)
Conformational disorders are involved in various neurodegenerative diseases. Reactive oxygen species (ROS) are the major contributors to neurodegenerative disease; however, ROS that affect the structural changes in misfolded disease proteins have yet to be well characterized. Here we demonstrate that
Giulia Dell'Omo et al.
British journal of cancer, 120(5), 537-546 (2019-02-12)
Nonsteroidal anti-inflammatory drugs (NSAIDs) have been proposed as chemopreventive agents for many tumours; however, the mechanism responsible for their anti-neoplastic activity remains elusive and the side effects due to cyclooxygenase (COX) inhibition prevent this clinical application. Molecular biology, in silico
Peter J Elliott et al.
Current opinion in investigational drugs (London, England : 2000), 9(4), 371-378 (2008-04-09)
Sirtuins represent a novel family of enzymes that are collectively well situated to help regulate nutrient sensing and utilization, metabolic rate and ultimately metabolic disease. Activation of one of these enzymes, SIRT1, leads to enhanced activity of multiple proteins, including
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