Recombinant HumanNAD-dependent protein lipoamidase sirtuin-4, mitochondrial (SIRT4)

Code CSB-YP897587HU
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Source Yeast
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Code CSB-EP897587HU
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Source E.coli
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Code CSB-EP897587HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP897587HU
MSDS
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Source Baculovirus
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Code CSB-MP897587HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
SIRT4
Uniprot No.
Alternative Names
MGC130046; MGC130047; MGC57437; NAD dependent deacetylase sirtuin 4; NAD dependent protein deacetylase sirtuin 4; NAD-dependent ADP-ribosyltransferase sirtuin-4; NAD-dependent protein deacetylase sirtuin-4; NAD-dependent protein lipoamidase sirtuin-4, mitochondrial; Regulatory protein SIR2 homolog 4; Silent mating type information regulation 2 homolog; Sir 2 like 4; SIR 2 like protein 4; Sir2 like 4; SIR2 like protein 4; SIR2-like protein 4; SIR2L 4; SIR2L4; SIR4_HUMAN; SIRT 4; Sirt4; Sirtuin (silent mating type information regulation 2 homolog) 4; Sirtuin (silent mating type information regulation 2 homolog) 4 (S. cerevisiae); Sirtuin 4; Sirtuin type 4; Sirtuin-4; Sirtuin4
Species
Homo sapiens (Human)
Expression Region
29-314
Target Protein Sequence
IG LFVPASPPLD PEKVKELQRF ITLSKRLLVM TGAGISTESG IPDYRSEKVG LYARTDRRPI QHGDFVRSAP IRQRYWARNF VGWPQFSSHQ PNPAHWALST WEKLGKLYWL VTQNVDALHT KAGSRRLTEL HGCMDRVLCL DCGEQTPRGV LQERFQVLNP TWSAEAHGLA PDGDVFLSEE QVRSFQVPTC VQCGGHLKPD VVFFGDTVNP DKVDFVHKRV KEADSLLVVG SSLQVYSGYR FILTAWEKKL PIAILNIGPT RSDDLACLKL NSRCGELLPL IDPC
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Acts as NAD-dependent protein lipoamidase, ADP-ribosyl transferase and deacetylase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. 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. 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. Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1:PPARA interaction probably through the regulation of NAD(+) levels. Down-regulates insulin secretion.
Gene References into Functions
  1. structural model of a complex of human Sirt4 and GDH in order to elucidate the molecular mechanism underlying the ADP-ribosylation of GDH by Sirt4 PMID: 29571013
  2. we propose that the SIRT4-OPA1 axis is causally linked to mitochondrial dysfunction and altered mitochondrial dynamics that translates into aging-associated decreased mitophagy based on an unbalanced mitochondrial fusion/fission cycle. PMID: 29081403
  3. SIRT4 protein levels in endometrioid adenocarcinoma were markedly lower than its non-neoplastic tissue counterpart (P< 0.001). PMID: 28582846
  4. Protein levels of SIRT 4 were significantly higher in HUVECs from HELLP pregnancies compared to control after 60 and 120 minutes of hypoxia. PMID: 27651178
  5. we found that knock-out of mitochondrial sirtuin sir-2.3, homologous to mammalian SIRT4, is protective in both chemical ischemia and hyperactive channel induced necrosis. This work suggests a deleterious role of SIRT4 during ischemic processes in mammals that must be further investigated PMID: 28820880
  6. miR-15b is a negative regulator of stress-induced SIRT4 expression, thereby counteracting senescence associated mitochondrial dysfunction and regulating the SASP and possibly organ aging, such as photoaging of human skin. PMID: 26959556
  7. SIRT4 overexpression inhibits the proliferation of colorectal cancer cells in vitro and in vivo. PMID: 26986234
  8. Thus, these results suggest that SIRT4 has essential roles in stress resistance and may be an important therapeutic target for cancer treatment. PMID: 26775843
  9. SIRT4 behaves as a tumor suppressor at the human tissue protein level. PMID: 26054687
  10. Overexpression of SIRT4 attenuated inflammation mediators in umbilical vein endothelial cells. PMID: 25331589
  11. SIRT4 has a tumour-suppressive function and may serve as a novel therapeutic target in colorectal cancer. PMID: 26086877
  12. Serum Sirt4 was inversely related to anthropometric and metabolic parameters and positively related to peak GH and IGF-1. PMID: 25466907
  13. C-terminal-binding protein (CtBP) was found to have an essential role in promoting glutaminolysis by directly repressing the expression of SIRT4. PMID: 25633289
  14. This study demonstrated that SIRT4 upregulation in the liver of non-alcoholic fatty liver disease patients. PMID: 25361925
  15. Until now, a mammalian cellular lipoamidase has not been characterized; this study discovered that SIRT4 can function with this enzymatic capacity in the mitochondria, and that PDH is a biological substrate; compared to its catalytic efficiency for deacetylation, SIRT4 exhibits far superior enzymatic activity for lipoyl- and biotinyl-lysine modifications. PMID: 25525879
  16. The present study shows low circulating levels of SIRT4 in obese patients with nonalcoholic fatty liver disease. PMID: 25045415
  17. regulates ATP levels via ANT2 and a feedback loop involving AMPK PMID: 24296486
  18. these results highlight the tumor-suppressive role of SIRT4 in Myc-induced B cell lymphoma and suggest that SIRT4 may be a potential target against Myc-induced and/or glutamine-dependent cancers. PMID: 24368766
  19. Study shows that mTORC1 promotes glutamine anaplerosis by activating glutamate dehydrogenase (GDH). This regulation requires transcriptional repression of SIRT4, the mitochondrial-localized sirtuin that inhibits GDH. Mechanistically, mTORC1 represses SIRT4 by promoting the proteasome-mediated destabilization of cAMP-responsive element binding 2. PMID: 23663782
  20. there is a negative correlation between SIRTs 1 and 4 and fasting plasma glucose, a positive correlation between SIRT4 mRNA levels and triglyceride/lipoprotein a levels, and a negative correlation between SIRT4 mRNA levels and HDL PMID: 21556116
  21. mitochondrial SIRT4 has a role in the regulation of insulin secretion PMID: 17715127

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Subcellular Location
Mitochondrion matrix.
Protein Families
Sirtuin family, Class II subfamily
Tissue Specificity
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.
Database Links

HGNC: 14932

OMIM: 604482

KEGG: hsa:23409

STRING: 9606.ENSP00000202967

UniGene: Hs.50861

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