IVD cDNA ORF Clone in Cloning Vector, Mouse

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IVD cDNA ORF Clone in Cloning Vector, Mouse: General Information

Gene
Species
Mouse
NCBI Ref Seq
RefSeq ORF Size
1275 bp
Sequence Description
Identical with the Gene Bank Ref. ID sequence except for the point mutations: 267C/T,732G/A,891G/A,933G/A not causing the amino acid variation.
Description
Full length Clone DNA of Mouse isovaleryl coenzyme A dehydrogenase
Plasmid
Vector
Sequencing Primers
M13-47 and RV-M
Quality Control
The plasmid is confirmed by full-length sequencing.
Screening
Antibiotic in E.coli
Ampicillin
Storage & Shipping
Shipping
Each tube contains lyophilized plasmid.
Storage
The lyophilized plasmid can be stored at ambient temperature for three months.

IVD cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

IVD cDNA ORF Clone in Cloning Vector, Mouse: Alternative Names

1300016K07Rik cDNA ORF Clone, Mouse; 6720455E18Rik cDNA ORF Clone, Mouse; AI463340 cDNA ORF Clone, Mouse

IVD Background Information

Isovaleryl-CoA dehydrogenase, also known as IVD, plays an essential role in processing proteins obtained from the diet. The body breaks down proteins from food into smaller parts called amino acids. Amino acids can be further processed to provide energy for growth and development. Isovaleryl-CoA dehydrogenase helps process a particular amino acid called leucine. Specifically, isovaleryl-CoA dehydrogenase is responsible for the third step in the breakdown of leucine. This step is a chemical reaction that converts a molecule called isovaleryl-CoA to another molecule, 3-methylcrotonyl-CoA. Additional chemical reactions convert 3-methylcrotonyl-CoA into molecules that are used for energy.
Full Name
isovaleryl-CoA dehydrogenase
References
  • BACHHAWAT BK, et al. (1956) Enzymatic carboxylation of beta-hydroxyisovaleryl coenzyme A. J Biol Chem. 219(2):539-50.
  • Ikeda Y, et al. (1983) Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria. J Biol Chem. 258(2):1077-85.
  • Tanaka K, et al. (1966) Enzymatic carboxylation of beta-hydroxyisovaleryl coenzyme A. J Biol Chem. 219(2):539-50.
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