Recombinant Human Acetyl-Coa Carboxylase 1 (ACACA) Protein (His)

Name: Recombinant Human Acetyl-Coa Carboxylase 1 (ACACA) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00264P
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 Acetyl-Coa Carboxylase 1 (ACACA) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13085
Target Symbol	ACACA
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	SMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMYGVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQMNRIDTGWLDRLI
Expression Range	78-617aa
Protein Length	Partial
Mol. Weight	67.1 kDa
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	Cytosolic enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty acid biosynthesis. This is a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA.
Subcellular Location	Cytoplasm, cytosol.
Database References	HGNC: 84 OMIM: 200350 KEGG: hsa:31 STRING: 9606.ENSP00000344789 UniGene: PMID: 29899443 These data showed that ACC1 gene (ACACA) expression was twofold greater in HCC compared to non-cancerous liver. PMID: 28290443 the present studies report for the first time a role of ACC1 in suppressing breast cancer migration and invasion by an fatty acid synthesis-independent, but acetyl-CoA-dependent, impact on the epithelial-mesenchymal transition programs in breast tumor cells and its subsequent importance for tumor invasion and recurrence. PMID: 29056512 the presence of an internal ribosome entry site in the ACC1 5' UTR allows ACC1 mRNA translation in conditions that are inhibitory to cap-dependent translation. PMID: 29343429 of ACCs decreased polyunsaturated fatty acid (PUFA) concentrations in liver due to reduced malonyl-CoA, which is required for elongation of essential fatty acids. PMID: 28768177 Inhibition of Acetyl-CoA Carboxylase 1 (ACC1) and 2 (ACC2) Reduces Proliferation and De Novo Lipogenesis of EGFRvIII Human Glioblastoma Cells PMID: 28081256 Cetuximab-mediated activation of AMPK and subsequent phosphorylation and inhibition of ACC is followed by a compensatory increase in total ACC, which rewires cancer metabolism from glycolysis-dependent to lipogenesis-dependent. PMID: 27693630 acetyl-CoA carboxylase 1 and senescence regulation in human fibroblasts involves oxidant mediated p38 MAPK activation PMID: 27983949 ACC1 and ACLY regulate the levels of ETV4 under hypoxia via increased alpha-ketoglutarate. These results reveal that the ACC1/ACLY-alpha-ketoglutarate-ETV4 axis is a novel means by which metabolic states regulate transcriptional output PMID: 26452058 Phospho-acetyl-CoA carboxylase protein expression correlates with tumor grade and the disease stage in gastric cancer. PMID: 24924473 ACAT1, ACACA, ALDH6A1 and MTHFD1 represent novel biomarkers in adipose tissue associated with type 2 diabetes in obese individuals. PMID: 25099943 ACACA may constitute a previously unrecognized target for novel anti-breast cancer stem cell therapies. PMID: 25246709 Single nucleotide polymorphisms in the ACACA and ACLY genes are associated with a relative change in plasma triglycierides following fish oil supplementation. PMID: 23886516 Exercise training increased AMPKalpha1 activity in older men, however, AMPKalpha2 activity, and the phosphorylation of AMPK, ACC and mTOR, were not affected PMID: 23000302 Metabolic regulation of invadopodia and invasion by acetyl-CoA carboxylase 1 and de novo lipogenesis. PMID: 22238651 IGF-1 reduced ACCalpha phosphorylation via an ATM/AMPK signaling pathway and suppressed ACCalpha expression through an ERK1/2 PMID: 21638027 three major enzymes of the pathway, FASN, ACC, and ACLY, are up-regulated in numerous tumor types. PMID: 21726077 Human cytomegalovirus infection induces an increase in ACC1 mRNA and protein expression. PMID: 21471234 Transient over-expression of CREB1 in HepG2 cells activates ACC1 PII promoter and induces the production of triacylglycerol in response to arachidonic acid (AA), indicating that the effect of AA on ACC1 is possibly regulated via CREB1. PMID: 19842072 data suggest that insulin and glucocorticoid have positive effects on both acetyl-CoA carboxylase alpha(ACC1) and beta(ACC2) gene transcription PMID: 20139635 show that MIG12, a 22 kDa cytosolic protein of previously unknown function, binds to ACC and lowers the threshold for citrate activation into the physiological range. PMID: 20457939 ACC was down-regulated in visceral adipose tissue from obese subjects, with and without diabetes mellitus type 2 PMID: 19543203 This study supports the hypothesis that the direct effects of some antipsychotics on hypertriglyceridemia may be at least partially mediated by the ACACA gene. PMID: 19846279 data suggest that cancer cells require active SCD1 to control the rate of glucose-mediated lipogenesis, and that when SCD1 activity is impaired cells downregulate SFA synthesis via AMPK-mediated inactivation of acetyl-CoA carboxylase PMID: 19710915 Human acetyl-CoA carboxylase 1 gene has three promoters and heterogeneity at the 5'-untranslated mRNA region PMID: 12810950 Transcription of ACC-alpha from at least three promoters and the potential to generate ACC-alpha isozymes with differential susceptibilities to phosphorylation indicate that the regulation of fatty acid synthesis in human tissues is likely to be complex PMID: 14643797 polymorphisms in acetyl-Coenzyme A carboxylase alpha is associated with breast cancer predisposition PMID: 15333468 BRCA1 affects lipogenesis through binding to P-ACCA, suggesting a new mechanism by which BRCA1 may exert a tumor suppressor function PMID: 16326698 the whole BRCA1 protein interacts with ACCA when phosphorylated on Ser1263. PMID: 16698035 a possible role of the ACC-alpha common sequence variants in susceptibility to breast cancer PMID: 17372234 observations provide complete information about the pattern and levels of LKB1 and p-ACC immunostaining in normal tissues and in lung tumors PMID: 17521700 the major mechanism of HER2-mediated induction of FASN and ACCalpha in the breast cancer cells used in this study is translational regulation primarily through the mTOR signaling pathway. PMID: 17631500 AKR1B10 regulates the stability of acetyl-CoA carboxylase-alpha and is a novel regulator of the biosynthesis of fatty acid, an essential component of the cell membrane, in breast cancer cells PMID: 18056116 biochemical analysis of human BRCA1 BRCT domains in complex with a phospho-peptide from human ACC1 PMID: 18452305 Differential activation of recombinant ACC1 and ACC2 by citrate is reported. PMID: 18455495 AMPK alpha2 activity, AMPK alpha2 Thr172 phosphorylation, and ACC-beta Ser222 phosphorylation were increased immediately after exercise. These increases had all returned to basal levels at 3 and 24 h after exercise. PMID: 18614941 Data suggest that increased expression of malonyl CoA decarboxylase, and the decreased expression of acetyl CoA carboxylase and 5'-AMP activated protein kinase are important regulators of the maturation of fatty acid oxidation in the newborn human heart. PMID: 18614968 The interaction between BRCA1 and acetyl-CoA-carboxylase is regulated during cell cycle progression. PMID: 19061860 Data show that kidney bean husk extract exhibited antitumor effects accompanied by the increase in p-AMPK and p-Acc as well as antitumor proteins p53 and p21. PMID: 19723093

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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.