Recombinant Human 1-Acylglycerol-3-Phosphate O-Acyltransferase Abhd5 (ABHD5) Protein (His-SUMO)

Name: Recombinant Human 1-Acylglycerol-3-Phosphate O-Acyltransferase Abhd5 (ABHD5) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04131P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human 1-Acylglycerol-3-Phosphate O-Acyltransferase Abhd5 (ABHD5) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8WTS1
Target Symbol	ABHD5
Synonyms	1-acylglycerol-3-phosphate O-acyltransferase ABHD5; ABHD5; ABHD5_HUMAN; Abhydrolase domain containing 5; Abhydrolase domain containing protein 5; Abhydrolase domain-containing protein 5; CDS; CGI 58; CGI58; CGI58 protein; IECN2; Lipid droplet-binding protein CGI-58; MGC8731; NCIE2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	AAEEEEVDSADTGERSGWLTGWLPTWCPTSISHLKEAEEKMLKCVPCTYKKEPVRISNGNKIWTLKFSHNISNKTPLVLLHGFGGGLGLWALNFGDLCTNRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALGLDKMILLGHNLGGFLAAAYSLKYPSRVNHLILVEPWGFPERPDLADQDRPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGKMHPDIPVSVIFGARSCIDGNSGTSIQSLRPHSYVKTIAILGAGHYVYADQPEEFNQKVKEICDTVD
Expression Range	2-349aa
Protein Length	Full Length of Mature Protein
Mol. Weight	55.0kDa
Research Area	Cancer
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	Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors. Functions in phosphatidic acid biosynthesis. May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2. Involved in keratinocyte differentiation. Regulates lipid droplet fusion.
Subcellular Location	Cytoplasm. Lipid droplet. Cytoplasm, cytosol.
Protein Families	Peptidase S33 family, ABHD4/ABHD5 subfamily
Database References	HGNC: 21396 OMIM: 275630 KEGG: hsa:51099 STRING: 9606.ENSP00000390849 UniGene: PMID: 28877685 Prebinding CGI-58 with PI(3)P or PI(5)P did not alter its coactivation of ATGL in vitro. In summary, purified recombinant CGI-58 that is functional as an ATGL coactivator lacks LPAAT activity. PMID: 24879803 It is clear that CGI-58 can regulate TAG hydrolysis by activating the major TAG hydrolase adipose triglyceride lipase (ATGL), yet CGI-58 can also regulate lipid metabolism via mechanisms that do not involve ATGL. PMID: 28827091 ABHD5 possesses a PNPLA2-independent function in regulating autophagy and tumorigenesis. PMID: 27559856 These results indicate that HCV taps into the lipid droplet triglyceride reservoir usurping ABHD5 lipase cofactor function PMID: 27124600 Case Report: novel ABHD5 mutation, c.838C > T (p.Arg280), in trans with p.Arg234 in a Chinese patient with very mild Dorfman-Chanarin syndrome. PMID: 26547112 Authors show that rat ATGL, coactivated by rat CGI-58, efficiently hydrolyzes triglycerides and retinyl ester. PMID: 26330055 novel ABHD5 truncating variant in a twenty nine month old female child, who presented with icthyosiform erythroderma. PMID: 26353074 simultaneous tryptophan alanine permutations in both arms abolish localization and activity of CGI-58 as opposed to tryptophan substitutions that occur in only one arm. PMID: 26350461 this study presents clinical and molecular data of four affected relatives with Chanarin-Dorfman syndrome homozygous for a N209X mutation in ABHD5, and provides a short review by comparing patients with N209X homozygous mutations to patients with other ABHD5 mutations. PMID: 25682902 PLIN5 was significantly colocated with ATGL, mitochondria and CGI-58, indicating a close association between the key lipolytic effectors in resting skeletal muscle. PMID: 25054327 -mediated phosphorylation of CGI-58 is required for dispersion of CGI-58 from perilipin 1A-coated lipid droplets PMID: 25421061 Abhd5 expression falls substantially and correlates negatively with malignant features in human colorectal cancer. PMID: 25482557 Findings indicate a molecular mechanisms by which lysophosphatidic acid acyltransferase CGI-58 regulates lipid homeostasis. PMID: 25315780 A report of two Chanarin-Dorfman syndrome sisters with severe steatohepatitis and decompensated cirrhosis due to steatohepatitis in whom the clinical presentation developed due to a new mutation in ABHD5 gene. PMID: 22245374 an important metabolic function of CGI-58 in skeletal muscle PMID: 22383684 A novel nonsense mutation of ABHD5 is reported in a consanguineous Afgani family with 4 sibs with Dorfman Chanarin syndrome; the mutation leads to protein truncation by 14 AAs; findings include liver cirrhosis, corneal opacities,tessellated fundus PMID: 22373837 the C terminus sequesters ABHD5 and thus inhibits basal ATGL activity PMID: 21757733 First report of large genomic deletions in the ABHD5 gene in Chanarin-Dorfman syndrome patients from Mediterranean countries. PMID: 21122093 analysis of novel mutations in the ABHD5 gene in Chanarin-Dorfman syndrome (CDS) patients PMID: 20307695 CGI-58 not only facilitates triglyceride lipolysis, but also provides fatty acid for esterification of ceremide leading to acylceremides PMID: 20520629 ABDH5 gene mutation is found in patients diagnosed with Chanarin Dorfman syndrome. PMID: 15967942 CGI-58 interacts with adipose triglyceride lipase, stimulating its TG hydrolase activity up to 20-fold PMID: 16679289 CGI-58 facilitates lipolysis in cooperation with perilipin and other factors, including lipases PMID: 17308334 analysis of a novel S115G mutation of CGI-58 in a Turkish patient with Dorfman-Chanarin syndrome [case report] PMID: 17495960 Deficient in lipid storage diseases. PMID: 17631826 These data enriches the list of CGI-58 mutations associated with Chanarin-Dorfman syndrome and confirms the clinical and allelic heterogeneity of this disease, especially the inconsistent muscle involvement. PMID: 18339307 CGI-58, the causative gene for Chanarin-Dorfman syndrome, mediates acylation of lysophosphatidic acid PMID: 18606822 CGI-58 is expressed and packaged into lamellar granules (LG) during keratinization and likely plays crucial role(s) in keratinocyte differentiation and LG lipid metabolism, contributing to skin lipid barrier formation. PMID: 18832586 Chanarin-Dorfman syndrome: deficiency in CGI-58, a lipid droplet-bound coactivator of lipase. (Review) PMID: 19061969 review summarizes recent findings with the goal of relating structural variants of ATGL and CGI-58 to functional consequences in lipid metabolism [review] PMID: 19401457 mutational analysis in Chanarin-Dorfman syndrome PMID: 11590543

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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.