Recombinant Mouse Nad-Dependent Protein Deacylase Sirtuin-5, Mitochondrial (SIRT5) Protein (His&Myc)

Name: Recombinant Mouse Nad-Dependent Protein Deacylase Sirtuin-5, Mitochondrial (SIRT5) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01689P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Mouse Nad-Dependent Protein Deacylase Sirtuin-5, Mitochondrial (SIRT5) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8K2C6
Target Symbol	SIRT5
Synonyms	Regulatory protein SIR2 homolog 5 SIR2-like protein 5
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	SSNMADFRKCFANAKHIAIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPQAFARNPSQVWEFYHYRREVMRSKEPNPGHLAIAQCEARLRDQGRRVVVITQNIDELHRKAGTKNLLEIHGTLFKTRCTSCGTVAENYRSPICPALAGKGAPEPETQDARIPVDKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDRELALCDLCLVVGTSSVVYPAAMFAPQVASRGVPVAEFNMETTPATDRFRFHFPGPCGKTLPEALAPHETERTS
Expression Range	37–310aa
Protein Length	Full Length of Mature Protein
Mol. Weight	37.6 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as Uox.
Subcellular Location	Mitochondrion. Cytoplasm, cytosol. Nucleus. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus.
Protein Families	Sirtuin family, Class III subfamily
Database References	KEGG: mmu:68346 STRING: 10090.ENSMUSP00000071048 UniGene: PMID: 27435822 findings reveal a key role for SIRT5 in maintaining cardiac oxidative metabolism under pressure overload to ensure survival PMID: 28972174 Deletion of Sirt5 in starved mouse embryonic fibroblasts increased levels of mitochondrial dynamics leading to mitochondrial accumulation of the pro-fission Drp1 and to mitochondrial fragmentation. PMID: 28340937 Our study uncovers a SIRT5-dependent mechanism that regulates cellular NADPH homeostasis and redox potential by promoting IDH2 desuccinylation and G6PD deglutarylation. PMID: 27113762 Data (including data from studies using knockout mice) suggest that SIRT5 is targeted to protein complexes on the inner mitochondrial membrane via affinity for cardiolipin to promote respiratory chain function, particularly Complex I and Complex II; SIRT5 expression is observed in inner mitochondrial membrane of periportal hepatocytes. PMID: 28458255 Data show that peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1alpha) overexpression significantly increased the expression of sirtuin 3 (SIRT3) and sirtuin 5 (SIRT5). PMID: 27052737 In the cochlea, the expression of SIRT1, 3, and 5 (both mRNA and protein) was decreased in the old mice PMID: 26472659 These findings establish that regulating heart metabolism and function is a major physiological function of lysine succinylation and SIRT5. PMID: 27051063 SIRT5 has a role in cellular metabolism with a multiple enzymatic activities PMID: 26208827 SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase PMID: 25811481 Pathway analysis identified glycolysis as the top SIRT5-regulated pathway. Importantly, glycolytic flux was diminished in primary hepatocytes from Sirt5(-/-) compared to WT mice. PMID: 26073543 Data indicated that SIRT5 ameliorates MPTP-induced nigrostriatal dopaminergic degeneration via preserving mitochondrial antioxidant capacity. PMID: 25541039 Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. PMID: 24703693 Loss of SIRT5 leads to accumulation of medium- and long-chain acylcarnitines and decreased beta-hydroxybutyrate production in vivo. PMID: 24315375 Sirt5 is likely to be dispensable for the metabolic homeostasis under the basal conditions. PMID: 24076663 We have isolated and characterized the murine sirt5 genomic sequence, which spans a region of 24,449 bp and which has one single genomic locus. PMID: 23673559 SIRT5 represses biochemical activity of, and cellular respiration through, two protein complexes identified as pyruvate dehydrogenase complex and succinate dehydrogenase. PMID: 23806337 The results suggest that SIRT5 activates UOX through deacetylation in mouse liver mitochondria. PMID: 23085393 These data indicate SIRT5 also has a role in the metabolic adaptation to fasting, high protein diet and calorie restriction. PMID: 20157539 Because ammonia generated during fasting is toxic, SIRT5 protein might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of CPS1. PMID: 20097174 results suggest that the SIRT3, SIRT4, and SIRT5 proteins exert distinct functions in mitochondria. PMID: 18054327 SIRT5 plays a pivotal role in ammonia detoxification and disposal by activating carbamoyl phosphate synthetase 1 PMID: 19410549

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.