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

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

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MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

SIRT4

Purity

>85% (SDS-PAGE)

Target Names

SIRT4

Uniprot NO.

Q9Y6E7

Species

Homo sapiens (Human)

Source

Yeast

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
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage

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.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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

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
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
SIRT4 protein levels in endometrioid adenocarcinoma were markedly lower than its non-neoplastic tissue counterpart (P< 0.001). PMID:28582846
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
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
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
SIRT4 overexpression inhibits the proliferation of colorectal cancer cells in vitro and in vivo. PMID:26986234
Thus, these results suggest that SIRT4 has essential roles in stress resistance and may be an important therapeutic target for cancer treatment. PMID:26775843
SIRT4 behaves as a tumor suppressor at the human tissue protein level. PMID:26054687
Overexpression of SIRT4 attenuated inflammation mediators in umbilical vein endothelial cells. PMID:25331589
SIRT4 has a tumour-suppressive function and may serve as a novel therapeutic target in colorectal cancer. PMID:26086877
Serum Sirt4 was inversely related to anthropometric and metabolic parameters and positively related to peak GH and IGF-1. PMID:25466907
C-terminal-binding protein (CtBP) was found to have an essential role in promoting glutaminolysis by directly repressing the expression of SIRT4. PMID:25633289
This study demonstrated that SIRT4 upregulation in the liver of non-alcoholic fatty liver disease patients. PMID:25361925
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
The present study shows low circulating levels of SIRT4 in obese patients with nonalcoholic fatty liver disease. PMID:25045415
regulates ATP levels via ANT2 and a feedback loop involving AMPK PMID:24296486
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
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
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
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

UNIGENE: Hs.50861

KEGG: hsa:23409

STRING: 9606.ENSP00000202967

OMIM: 604482

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