SIRT1 Antibody (YA6327)
(Synonyms: SIRT1; SIR2L1; NAD-dependent protein deacetylase sirtuin-1; hSIRT1; Regulatory protein SIR2 homolog 1; SIR2-like protein 1; hSIR2)SIRT1 Antibody (YA6327) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to SIRT1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, IP, ELISA
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Reactivity :
Human, Rat
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Formulation:
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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IP
IP: Immunoprecipitation
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|---|---|---|---|---|---|
| Dilution Ratio | 1:100-200 | 1:1000-5000 | 1:200-1000 | 1:5000-20000 | 1:50-200 |
Product Details
SIRT1 Antibody (YA6327) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to SIRT1.
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Host Rabbit
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Clonality Monoclonal
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Species ReactivityHuman, Rat
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Observed Molecular WeightObserved band size: 130 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 81 kDa
Protein A
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
SIRT1 is a NAD\\+-dependent deacetylase that functions as a central regulator of cellular metabolism, stress responses, genomic stability, and aging through deacetylation of histones and multiple transcriptional regulators[1][2]. Mechanistically, SIRT1 integrates nutrient and energy signals with transcriptional programs that control mitochondrial biogenesis, fatty acid oxidation, glucose metabolism, autophagy, and cellular adaptation to metabolic stress[1][3]. Through coordinated interactions with metabolic signaling networks, SIRT1 contributes to maintenance of metabolic health across liver, skeletal muscle, adipose tissue, heart, and other organs[1]. In disease-related contexts, altered SIRT1 activity has been associated with aging, chronic inflammatory conditions, obesity, metabolic dysfunction, cardiovascular disorders, neurodegenerative diseases, and cancer-related processes, making it a widely used experimental target in translational research[2][4][5]. Compared with related sirtuin isoforms, SIRT1 is the most extensively characterized mammalian sirtuin and primarily mediates transcriptional regulation through deacetylation of nuclear histone and non-histone substrates, whereas other family members display distinct cellular localization and substrate preferences[1][2][4]. For experimental applications, SIRT1 activity can be modulated by small-molecule activators and inhibitors, and naturally occurring polyphenols such as resveratrol have been reported to activate SIRT1 in multiple model systems, providing useful tools for mechanistic studies of metabolism, inflammation, oxidative stress, and aging biology[3][4].
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Subcellular Localization
Nucleus, PML body; Cytoplasm; Nucleus; Cytoplasm; Mitochondrion
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Expression
Tissue_specificity:Broad expression
Induction:Up-regulated by methyl methanesulfonate (MMS) . In H293T cells by presence of rat calorie restriction (CR) serum -
Isoforms & Post-Translational Modification
Human (Q96EB6) has 2 isomers: Q96EB6-1: 81,681 Da (predicted); Q96EB6-2: 61,066 Da (predicted).
Methylated on multiple lysine residues.
Phosphorylated.
Proteolytically cleaved by cathepsin B upon TNF-alpha treatment to yield catalytic inactive but stable SirtT1 75 kDa fragment (75SirT1).
S-nitrosylated by GAPDH.
Acetylated at various Lys residues.
Ubiquitinated. -
Subunit
Interacts with XBP1 isoform 2 (PubMed:20955178). Found in a complex with PCAF and MYOD1. Interacts with FOXO1; the interaction deacetylates FOXO1, resulting in its nuclear retention and promotion of its transcriptional activity Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Interacts with HES1, HEY2 and PML. Interacts with RPS19BP1/AROS. Interacts with CCAR2 (via N-terminus); the interaction disrupts the interaction between SIRT1 and p53/TP53. Interacts with SETD7; the interaction induces the dissociation of SIRT1 from p53/TP53 and increases p53/TP53 activity. Interacts with MYCN, NR1I2, CREBZF, TSC2, TLE1, FOS, JUN, NR0B2, PPARG, NCOR, IRS1, IRS2 and NMNAT1. Interacts with HNF1A; the interaction occurs under nutrient restriction. Interacts with SUZ12; the interaction mediates the association with the PRC4 histone methylation complex which is specific as an association with PCR2 and PCR3 complex variants is not found. Interacts with BCL6; leads to a epigenetic repression of specific target genes. Interacts with CLOCK, BMAL1 and PER2 (By similarity). Interacts with PPARA; the interaction seems to be modulated by NAD(+) levels (PubMed:24043310). Interacts with NR1H3 and this interaction is inhibited in the presence of CCAR2. Interacts with CHEK2. Interacts with p53/TP53. Exhibits a preferential interaction with sumoylated CCAR2 over its unmodified form. Interacts with PACS2 (PubMed:29656858). Interacts with SIRT7 (By similarity). Interacts with PUS7 (PubMed:31451225). Interacts with TULP3 (PubMed:35397207). Interacts with MORN3; the interaction enhances the ubiquitination of p53/TP53 (PubMed:29681526)
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SwissProt ID
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Synonyms
SIRT1; SIR2L1; NAD-dependent protein deacetylase sirtuin-1; hSIRT1; Regulatory protein SIR2 homolog 1; SIR2-like protein 1; hSIR2
Documentation
References
[1]. Dijk W, et al. Regulation of lipoprotein lipase by Angptl4. Trends Endocrinol Metab. 2014 Mar;25(3):146-55. [Content Brief]
[2]. Zhao L, et al. Sirtuins and their Biological Relevance in Aging and Age-Related Diseases. Aging Dis. 2020 Jul 23;11(4):927-945. [Content Brief]
[3]. Chung S, et al. Regulation of SIRT1 in cellular functions: role of polyphenols. Arch Biochem Biophys. 2010 Sep 1;501(1):79-90. [Content Brief]
[4]. Carafa V, et al. Sirtuins and disease: the road ahead. Front Pharmacol. 2012 Jan 31;3:4. [Content Brief]
[5]. Herskovits AZ, et al. Sirtuin deacetylases in neurodegenerative diseases of aging. Cell Res. 2013 Jun;23(6):746-58. [Content Brief]
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