Recombinant Human SIRT4 protein is a Human Full Length protein, in the 1 to 314 aa range, expressed in Escherichia coli, with >70% purity and suitable for SDS-PAGE.
M K M S F A L T F R S A K G R W I A N P S Q P C S K A S I G L F V P A S P P L D P E K V K E L Q R F I T L S K R L L V M T G A G I S T E S G I P D Y R S E K V G L Y A R T D R R P I Q H G D F V R S A P I R Q R Y W A R N F V G W P Q F S S H Q P N P A H W A L S T W E K L G K L Y W L V T Q N V D A L H T K A G S R R L T E L H G C M D R V L C L D C G E Q T P R G V L Q E R F Q V L N P T W S A E A H G L A P D G D V F L S E E Q V R S F Q V P T C V Q C G G H L K P D V V F F G D T V N P D K V D F V H K R V K E A D S L L V V G S S L Q V Y S G Y R F I L T A W E K K L P I A I L N I G P T R S D D L A C L K L N S R C G E L L P L I D P C
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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).
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
Recombinant Human SIRT4 protein is a Human Full Length protein, in the 1 to 314 aa range, expressed in Escherichia coli, with >70% purity and suitable for SDS-PAGE.
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
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).
Belongs to the sirtuin family. Class II subfamily.
SIRT4 also known as Sirtuin 4 is a mitochondrial protein with a mass of approximately 36 kDa. It belongs to the sirtuin family of NAD+-dependent deacetylases. Unlike many other sirtuins SIRT4 does not function as a deacetylase; instead it exhibits ADP-ribosyltransferase activity. This activity regulates a range of mitochondrial functions. SIRT4 is expressed in various tissues including the liver pancreas and muscles where it plays different roles based on the tissue type.
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.
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.
SIRT4 links to metabolic conditions such as diabetes and metabolic syndrome. Dysregulation of SIRT4 activity can lead to impaired insulin secretion and glucose intolerance. Furthermore SIRT4's interaction with other sirtuins particularly SIRT1 suggests a functional interplay in protecting against metabolic stress and possibly influencing the development of these metabolic disorders.
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The putity of ab101713 was determined to be 90% by densitometry.
Approximate MWt: 62kDa
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