HPA022992
Anti-SIRT5 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab3
Synonym(e):
Anti-NAD-dependent deacetylase sirtuin-5, Anti-SIR2-like protein 5
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Alle Fotos(2)
About This Item
Empfohlene Produkte
Biologische Quelle
rabbit
Konjugat
unconjugated
Antikörperform
affinity isolated antibody
Antikörper-Produkttyp
primary antibodies
Klon
polyclonal
Produktlinie
Prestige Antibodies® Powered by Atlas Antibodies
Form
buffered aqueous glycerol solution
Speziesreaktivität
human
Methode(n)
immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:20-1:50
Immunogene Sequenz
AKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQN
UniProt-Hinterlegungsnummer
Versandbedingung
wet ice
Lagertemp.
−20°C
Posttranslationale Modifikation Target
unmodified
Angaben zum Gen
human ... SIRT5(23408)
Allgemeine Beschreibung
The gene SIRT5 (sirtuin 5) is mapped to human chromosome 6p23. It is mainly expressed in brain, testis, heart muscle cells, and lymphoblasts. SIRT5 belongs to the sirtuins family of NAD (nicotinamide adenine dinucleotide)-dependent lysine deacylases. The protein is present in the mitochondria.
Immunogen
NAD-dependent deacetylase sirtuin-5 recombinant protein epitope signature tag (PrEST)
Anwendung
All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.
The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.
The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.
Biochem./physiol. Wirkung
Sirtuins (SIRTs) are responsible for the removal of acetyl groups from modified lysine residues in proteins. SIRT5 uses malonyllysine, succinyllysine, and glutaryllysine as substrates. It can also enhance mitochondrial respiration and cellular metabolism in the presence of excess glucose. SIRT5 is involved in the activation of SOD1 (superoxide dismutase 1) by desuccinylation, leading to elimination of reactive oxygen species. It also participates in caloric restriction effects by deacetylation of CPS1 (carbamoyl phosphate synthetase 1).
Leistungsmerkmale und Vorteile
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Verlinkung
Corresponding Antigen APREST73828
Physikalische Form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Rechtliche Hinweise
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
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Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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Anja Schuetz et al.
Structure (London, England : 1993), 15(3), 377-389 (2007-03-16)
Sirtuins are NAD(+)-dependent protein deacetylases and are emerging as molecular targets for the development of pharmaceuticals to treat human metabolic and neurological diseases and cancer. To date, several sirtuin inhibitors and activators have been identified, but the structural mechanisms of
Michelle Barbi de Moura et al.
PloS one, 9(8), e106028-e106028 (2014-08-29)
SIRT3, SIRT4, and SIRT5 are mitochondrial deacylases that impact multiple facets of energy metabolism and mitochondrial function. SIRT3 activates several mitochondrial enzymes, SIRT4 represses its targets, and SIRT5 has been shown to both activate and repress mitochondrial enzymes. To gain
Frank Fischer et al.
PloS one, 7(9), e45098-e45098 (2012-10-03)
Sirtuins are protein deacylases regulating metabolism and aging processes, and the seven human isoforms are considered attractive therapeutic targets. Sirtuins transfer acyl groups from lysine sidechains to ADP-ribose, formed from the cosubstrate NAD(+) by release of nicotinamide, which in turn
Repression of p53 function by SIRT5-mediated desuccinylation at Lysine 120 in response to DNA damage.
Liu, et al.
Cell Death and Differentiation, 29, 722-736 (2023)
D Guan et al.
Cell death & disease, 5, e1340-e1340 (2014-07-18)
The promyelocytic leukemia protein (PML) is a tumor suppressor that is expressed at a low level in various cancers. Although post-translational modifications including SUMOylation, phosphorylation, and ubiquitination have been found to regulate the stability or activity of PML, little is
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