SIRT4 / Sirtuin 4 Antibody (C-Terminus)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
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Primary Accession | Q9Y6E7 |
Reactivity | Human |
Host | Goat |
Clonality | Polyclonal |
Calculated MW | 35kDa |
Dilution | IHC-P (2.5 µg/ml), WB (1-3 µg/ml), |
Gene ID | 23409 |
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Other Names | NAD-dependent protein deacetylase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161}, 3.5.1.- {ECO:0000255|HAMAP-Rule:MF_03161}, NAD-dependent ADP-ribosyltransferase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161}, 2.4.2.- {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 | Human SIRT4. |
Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
Precautions | SIRT4 / Sirtuin 4 Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SIRT4 {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000312|HGNC:HGNC:14932} |
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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. |
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Background
Acts both as NAD-dependent protein ADP-ribosyl transferase and NAD-dependent protein deacetylase. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. 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. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. 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. Down-regulates insulin secretion.
References
Frye R.A.,et al.Biochem. Biophys. Res. Commun. 260:273-279(1999).
Scherer S.E.,et al.Nature 440:346-351(2006).
Haigis M.C.,et al.Cell 126:941-954(2006).
Ahuja N.,et al.J. Biol. Chem. 282:33583-33592(2007).
Michishita E.,et al.Mol. Biol. Cell 16:4623-4635(2005).
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