Recombinant Human SIRT5 protein is a Human Full Length protein, in the 1 to 310 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, WB.
>95% SDS-PAGE
Escherichia coli
GST tag N-Terminus
SDS-PAGE, WB
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX.
SIR2L5, SIR2L5, SIRT5, Regulatory protein SIR2 homolog 5, SIR2-like protein 5
Recombinant Human SIRT5 protein is a Human Full Length protein, in the 1 to 310 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, WB.
>95% SDS-PAGE
Escherichia coli
GST tag N-Terminus
SDS-PAGE, WB
No
No
Human
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.307% Glutathione, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00292% EDTA, 0.00174% PMSF
Full Length
60 kDa
1 to 310
Recombinant
GST tag N-Terminus
Liquid
The purity was determined to be >95% by densitometry
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX.
Belongs to the sirtuin family. Class III subfamily.
Mitochondrion matrix, Mitochondrion intermembrane space, Nucleus, Mitochondrion
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
SIRT5 also known as Sirtuin 5 is a mitochondrial protein with enzymatic activity as a lysine desuccinylase demalonylase and deglutarylase. It has a molecular mass of approximately 34 kDa. This protein is expressed highly in tissues with high metabolic activity like the liver heart and brain where it participates in regulating energy metabolism. The activity of SIRT5 affects cellular processes by removing post-translational modifications from lysine residues modulating proteins' functions and interactions in these tissues.
SIRT5 functions as an important regulator of mitochondrial metabolism and influences cellular energy homeostasis. It is not part of larger complexes but it interacts with various metabolic enzymes to control their function. Through its deacylase activity SIRT5 affects the urea cycle and fatty acid oxidation by modifying key enzymes involved in these processes. Its role in maintaining a balance in energy production and consumption highlights its importance in cellular metabolism.
SIRT5 is involved in both the tricarboxylic acid (TCA) cycle and the regulation of reactive oxygen species (ROS). Within the TCA cycle SIRT5 desuccinylates and activates enzymes like citrate synthase enhancing the cycle's efficiency. In regulating ROS SIRT5 reduces oxidative stress by affecting enzymes such as superoxide dismutase 2 (SOD2). Its interaction with these pathways and proteins reflects its role in maintaining metabolic health and cellular integrity.
Alterations in SIRT5 levels have been connected to metabolic diseases such as obesity and neurodegenerative disorders like Alzheimer's disease. In obesity SIRT5 dysregulation can lead to inefficient metabolic processes and energy imbalance. In Alzheimer’s decreased SIRT5 activity may contribute to increased mitochondrial oxidative stress implicated in disease progression. These connections highlight SIRT5’s significance in both metabolic and neurodegenerative contexts linking with proteins like AMPK in obesity and tau proteins in Alzheimer's disease.
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SDS-PAGE showing ab101133 at approximately 60kDa.
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