Recombinant Phospho-SIRT1(Ser27) Monoclonal Antibody (AN302088L)
For research use only.
| Verified Samples |
Verified Samples in WB: HEK-293+CA, Jurkat+CA Verified Samples in IF: HEK-293+CalyculinA (-) (+) |
| Dilution | WB 1:500-1:1000, IF 1:50 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB, IF |
| Clonality | Monoclonal;Recombinant |
| Immunogen | phosphorylated human SIRT1(Ser27) peptide |
| Abbre | Phospho-SIRT1(Ser27) |
| Synonyms | SIR, HST, SIRT, Hsir, homolog-like, SIR2 like protein, Regulatory protein SIR2 homolog, NAD-dependent deacetylase sirtuin, Sirtuin (silent mating type information regulation 2 homolog), SIR2L, Hsirt, 75SirT, sirtuin, SIRT1, SIR2, SIR2L1, SIR2alpha, sirtuin 1, 75SirT1, Hsir2, Hsirt1, HST2, S.cerevisiae, NAD-dependent deacetylase sirtuin-1, Regulatory protein SIR2 homolog 1, SIR2 like protein 1, homolog-like 1, SirtT1 75 kDa fragment, Sirtuin (silent mating type information regulation 2 homolog) 1, SIR2, SIR2alpha, SIR2L1, sirtuin 1, homolog of, NAD dependent deacetylase sirtuin 1, NAD dependent protein deacetylase sirtuin 1, OTTHUMP00000198111, OTTHUMP00000198112, S. cerevisiae, SIR1, SIR2 like 1, SIR2-like protein 1, Sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae), Sirtuin type 1 |
| Swissprot | |
| Calculated MW | 82 kDa |
| Observed MW |
120 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cytoplasm, Nucleus, Mitochondrion |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Cell Biology, Epigenetics and Nuclear Signaling, Microbiology, Tags & Cell Markers, Metabolism |
| Clone No. | A812 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | SIRT1 is a member of the Silent Information Regulator2 (SIR2) family, which is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging. SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include acetylated p53, p300, Ku70, forkhead (FoxO) transcription factors, PPARγ, and the PPARγ coactivator-1α (PGC-1α) protein. SirT1 deacetylase activity is inhibited by nicotinamide and activated by resveratrol. In addition, SirT1 activity may be regulated by phosphorylation, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined. |
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Unconjugated
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