Active Recombinant Human ACACB protein, His-tagged
Cat.No. : | ACACB-1849H |
Product Overview : | Recombinant full length Human ACACB fused with His tag at N-terminal was expressed in Insect cells. |
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Description : | Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine-palmitoyl-CoA transferase I, the rate-limiting step in fatty acid uptake and oxidation by mitochondria. ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. There is evidence for the presence of two ACC-beta isoforms. |
Source : | Insect cells |
Species : | Human |
Tag : | His |
Form : | 40 mM Tris pH 8.0, 110 mM NaCl, 2.2 mM KCl, 0.04% Tween-20, 20% glycerol, and 3 mM DTT. |
Bio-activity : | ≥41 pmoles/min/µg |
Molecular Mass : | 277 kDa |
Purity : | >56% |
Applications : | Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. |
Storage : | >6 months at –80 centigrade. Avoid freeze/thaw cycles. |
Concentration : | 0.07 mg/ml |
Gene Name : | ACACB acetyl-CoA carboxylase beta [ Homo sapiens ] |
Official Symbol : | ACACB |
Synonyms : | ACACB; acetyl-CoA carboxylase beta; acetyl Coenzyme A carboxylase beta; acetyl-CoA carboxylase 2; ACC2; ACCB; acetyl CoA carboxylase 2; HACC275; ACC-beta; acetyl-Coenzyme A carboxylase beta; |
Gene ID : | 32 |
mRNA Refseq : | NM_001093 |
Protein Refseq : | NP_001084 |
MIM : | 601557 |
UniProt ID : | O00763 |
Chromosome Location : | 12q24.1 |
Pathway : | AMPK signaling, organism-specific biosystem; Adipocytokine signaling pathway, organism-specific biosystem; Adipocytokine signaling pathway, conserved biosystem; ChREBP activates metabolic gene expression, organism-specific biosystem; Fatty Acid Biosynthesis, organism-specific biosystem; Fatty acid biosynthesis, organism-specific biosystem; Fatty acid biosynthesis, conserved biosystem; |
Function : | ATP binding; acetyl-CoA carboxylase activity; biotin carboxylase activity; ligase activity; metal ion binding; nucleotide binding; protein binding; |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (10)
Ask a questionThe downstream targets of acetyl-CoA carboxylase beta protein include fatty acid synthase and other enzymes involved in lipid synthesis.
Acetyl-CoA carboxylase beta protein is responsible for the carboxylation of acetyl-CoA, which is a key step in fatty acid synthesis.
Acetyl-CoA carboxylase beta protein has been implicated in the development of insulin resistance and metabolic diseases due to its role in lipid metabolism.
Acetyl-CoA carboxylase beta protein is regulated by various post-translational modifications and allosteric regulators.
Acetyl-CoA carboxylase beta protein is a multi-domain protein composed of several structural domains.
Acetyl-CoA carboxylase beta protein interacts with several other proteins involved in lipid metabolism, including fatty acid synthase and AMP-activated protein kinase.
Acetyl-CoA carboxylase beta protein plays a crucial role in fatty acid metabolism and lipid synthesis.
Acetyl-CoA carboxylase beta protein is expressed in various tissues, with the highest expression observed in the liver and adipose tissue.
Several genetic variants in the acetyl-CoA carboxylase beta gene have been associated with metabolic disorders such as obesity and type 2 diabetes.
Potential therapeutic targets for regulating acetyl-CoA carboxylase beta protein activity include small molecule inhibitors and modulators of its regulatory pathways.
Customer Reviews (2)
Write a reviewDemonstrates high selectivity and sensitivity in detecting protein-protein interactions in pull-down assays.
Provides accurate and reliable quantification of protein biomarkers in clinical samples.
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