Recombinant Human SIRT4 protein
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Recombinant Human SIRT4 protein is a Human Full Length protein, in the 1 to 314 aa range, expressed in Escherichia coli, with >70%, suitable for SDS-PAGE.
View Alternative Names
SIR2L4, SIRT4, NAD-dependent ADP-ribosyltransferase sirtuin-4, NAD-dependent protein biotinylase sirtuin-4, NAD-dependent protein deacetylase sirtuin-4, Regulatory protein SIR2 homolog 4, SIR2-like protein 4
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human SIRT4 protein (AB101713)
The putity of ab101713 was determined to be 90% by densitometry.
Approximate MWt : 62kDa
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
SIRT4 regulates energy metabolism and cellular stress responses. It plays key roles in the regulation of mitochondrial functions during fasting and impacts gluconeogenesis and fatty acid oxidation. SIRT4 inhibits glutamate dehydrogenase (GDH) affecting amino acid metabolism and insulin secretion. By acting in this capacity SIRT4 controls the flow of nutrients and energy homeostasis exhibiting its critical role in metabolic regulation.
Pathways
SIRT4 integrates into a broader metabolic network including the insulin signaling and AMPK pathways. It interacts with proteins like GDH and AMPK influencing mitochondrial energy output and stress response. This relationship places SIRT4 in an important position for maintaining energy balance and responding to cellular metabolic demands.
Specifications
Form
Liquid
General info
Function
Acts as a NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase (PubMed : 16959573, PubMed : 17715127, PubMed : 24052263, PubMed : 25525879). Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications (PubMed : 24052263, PubMed : 25525879). Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed : 25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity (PubMed : 16959573, PubMed : 17715127). Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1 : expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed : 16959573, PubMed : 17715127). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation (PubMed : 23663782). Acts as a tumor suppressor (PubMed : 23562301, PubMed : 23663782). Also acts as a NAD-dependent protein deacetylase : mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (By similarity). Does not seem to deacetylate PC (PubMed : 23438705). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation (PubMed : 24043310). Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels (PubMed : 24043310). Down-regulates insulin secretion (PubMed : 17715127).
Sequence similarities
Belongs to the sirtuin family. Class II subfamily.
Subcellular localisation
Mitochondrion matrix
Target data
Complementary Products
Product promise
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