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SIRT4 Antibody (C-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q9Y6E7
Clone Names 2081910
Additional Information
Gene ID 23409
Other Names NAD-dependent protein deacetylase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161}, 351- {ECO:0000255|HAMAP-Rule:MF_03161}, NAD-dependent ADP-ribosyltransferase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161}, 242- {ECO:0000255|HAMAP-Rule:MF_03161}, Regulatory protein SIR2 homolog 4 {ECO:0000255|HAMAP-Rule:MF_03161}, SIR2-like protein 4 {ECO:0000255|HAMAP-Rule:MF_03161}, SIRT4 {ECO:0000255|HAMAP-Rule:MF_03161}, SIR2L4
Target/Specificity The synthetic peptide sequence used to generate the antibody AP6243a was selected from the C-term region of human SIRT4 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name SIRT4 {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000312|HGNC:HGNC:14932}
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).
Cellular Location Mitochondrion matrix {ECO:0000255|HAMAP- Rule:MF_03161, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:17715127}
Tissue Location Detected in vascular smooth muscle and striated muscle. Detected in insulin-producing beta-cells in pancreas islets of Langerhans (at protein level). Widely expressed. Weakly expressed in leukocytes and fetal thymus.
Research Areas
Citations (0)
citation

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Background

SIRT4 is a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.

References

Frye, R.A., Biochem. Biophys. Res. Commun. 273(2):793-798 (2000).Frye, R.A., Biochem. Biophys. Res. Commun. 260(1):273-279 (1999).

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$ 277.78
Cat# BP6243a
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