Acot12 (GeneName), Acetyl-coenzyme A thioesterase (ProteinName), ACO12_RAT.
Product Name:
Rat Acot12/ Acetyl-coenzyme A thioesterase ELISA Kit
Cat.#:
-
Brand:
EIAab®
Regulatory Status:
Alternative:
Acyl-CoA thioester hydrolase 12, Cach, Cach1, Acyl-coenzyme A thioesterase 12, Acyl-CoA thioesterase 12, Cytoplasmic acetyl-CoA hydrolase 1, CACH-1
Detection Method:
ELISA
Specificity:
Natural and recombinant rat Acetyl-coenzyme A thioesterase
Sample Type:
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Sample Data:
Research Area:
-
- Data
- Citations
- Publication
- Sequence / 3D
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General Annotation
Sub Unit:
Homodimer or homotetramer.
Function:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (Probable). Acyl-coenzyme A thioesterase 12/ACOT12 preferentially hydrolyzes acetyl-CoA (PubMed:11322891).
Subcellular Location:
Cytoplasm
Cytosol
Database link
UniGene:
SMR:
STRING:
KEGG:
Pfam:
Uniprot:
This product has not yet been referenced specifically in any publications.
[1].
"Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase."
[2].
"Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score."
[5].
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
[6].
"Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase."
[7].
"Architecture of the human interactome defines protein communities and disease networks."
[8].
"Genome-wide association study of smoking behaviours among Bangladeshi adults."
[9].
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
[10].
"Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain."
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