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ATP-citrate synthase beta chain protein 1 (ACLB-1), Recombinant Protein
Cat: RP07245
Species: Arabidopsis thaliana (Mouse-ear cress)
Datasheet:
Product Info
Full Product Name
Recombinant Arabidopsis thaliana ATP-citrate synthase beta chain protein 1 (ACLB-1) , partial
Product Gene Name
ACLB-1 recombinant protein
Product Synonym Gene Name
ACLB-1
Purity
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Molecular Weight
65,814 Da
Storage
Store at -20℃. For long-term storage, store at -20℃ or -80℃. Store working aliquots at 4℃ for up to one week. Repeated freezing and thawing is not recommended.
Protein Family
ATP-citrate synthase beta chain protein
NCBI/Uniprot Data
NCBI Accession #
NP_001326324.1
NCBI GI #
1063709912
NCBI GenBank Nucleotide #
NM_001337675.1
NCBI GeneID
819845
NCBI Official Full Name
ATP-citrate lyase B-1
NCBI Official Symbol
ACLB-1
NCBI Official Synonym Symbols
ATP-citrate lyase B-1; T8E24.7; T8E24_7
NCBI Protein Information
ATP-citrate lyase B-1
NCBI Summary
One of the two genes encoding subunit B of the trimeric enzyme ATP Citrate lyase
UniProt Gene Name
ACLB-1
UniProt Synonym Gene Names
ATP-citrate synthase B-1
UniProt Protein Name
ATP-citrate synthase beta chain protein 1
UniProt Synonym Protein Names
ATP-citrate lyase B-1; Citrate cleavage enzyme B-1
UniProt Primary Accession #
Q9C522
UniProt Related Accession #
Q9C522
UniProt Comments
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains .
For research use only, not for clinical use.