SIRT4 recombinant protein

SIRT4 (GST-tagged), Human recombinant

Cat. Num. AAA844796

• Gene Names: SIRT4; SIR2L4
• Applications: SDS-Page
• Purity: >=95%
• Synonyms: SIRT4; SIRT4 (GST-tagged); Human recombinant; SIR2-like Protein 4; NAD-dependent ADP-ribosyltransferase Sirtuin 4; SIR2L4; Silent Information Regulator 4; Sirtuin 4; SIRT4 recombinant protein

• Host: E Coli
• Purity/Purification: >=95%
• Form/Format: 50 mM sodium phosphate, pH 7.2, 100 mM sodium chloride, 2.5 mM DTT, 20% glycerol.; Appearance: Liquid
• Sequence Length: 314

• Applicable Applications for SIRT4 recombinant protein: SDS-PAGE; HPLC
• Handling: Centrifuge the vial prior to opening.
• Preparation and Storage: At -80 degree C; Shelf Life: 9 months

Testing Data

Related Product Information for SIRT4 recombinant protein

Background: There are seven human sirtuins, also known as class III HDACs, which have been designated SIRT1 to SIRT7. Each is involved in various post-translational modifications by utilizing NAD dependent deacetylase and APD-ribosyltransferase activities. SIRT4 is a mitochondrial ADP-ribosyltransferase responsible for the transfer of ADP-ribose from NAD to specific substrates such as glutamate dehydrogenase (GDH). In caloric-sufficient conditions, SIRT4 ADP-ribosylates GDH, repressing its activity and correspondingly decreasing insulin secretion. There is some uncertainty about the relevance of sirtuin ribosyl transferase activity due to its very slow rate, which is about 500 times lower than the corresponding deacetylation reaction (for those that have been characterized). SIRT4 is found in many tissues, but is specifically enriched in the kidney, heart, brain, and liver.

Product Categories/Family for SIRT4 recombinant protein

Epigenetics; HDACs; HDACsEpigenetics; Recombinant ProteinsProteins and Enzymes; Animal-Free Origin (AOF) Recombinant Proteins & EnzymesProteins and Enzymes; Proteins and Enzymes (A-Z)

NCBI and Uniprot Product Information

• NCBI GI #: 6912662
• NCBI GeneID: 23409
• NCBI Accession #: NP_036372.1
• NCBI GenBank Nucleotide #: NM_012240.2
• UniProt Accession #: Q9Y6E7; O43346; Q32M33
• Molecular Weight: 61.9 kDa (NT GST Tag)
• NCBI Official Full Name: NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
• NCBI Official Synonym Full Names: sirtuin 4
• NCBI Official Symbol: SIRT4
• NCBI Official Synonym Symbols: SIR2L4
• NCBI Protein Information: NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
• UniProt Protein Name: NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
• Protein Family: NAD-dependent protein deacylase
• UniProt Gene Name: SIRT4
• UniProt Entry Name: SIR4_HUMAN

NCBI Description

This gene encodes 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. The protein encoded by this gene is included in class IV of the sirtuin family. [provided by RefSeq, Jul 2008]

Uniprot Description

SIRT4: NAD-dependent protein ADP-ribosyl transferase. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1. Inhibits GLUD1 enzyme activity. Down- regulates insulin secretion. Has no detectable protein deacetylase activity. Belongs to the sirtuin family. Class II subfamily.

Protein type: Mitochondrial; EC 2.4.2.-; Deacetylase; Tumor suppressor; EC 3.5.1.-

Chromosomal Location of Human Ortholog: 12q

Cellular Component: mitochondrion; mitochondrial matrix

Molecular Function: protein binding; zinc ion binding; NAD+ ADP-ribosyltransferase activity

Biological Process: protein amino acid ADP-ribosylation; chromatin silencing; glutamine metabolic process; positive regulation of lipid biosynthetic process; response to DNA damage stimulus; negative regulation of fatty acid oxidation; negative regulation of insulin secretion