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NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial (EMB1467), Recombinant Protein
Cat: RP08297
Species: Arabidopsis thaliana (Mouse-ear cress)
Datasheet:
Product Info
Full Product Name
Recombinant Arabidopsis thaliana NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial (EMB1467) , partial
Product Gene Name
EMB1467 recombinant protein
Product Synonym Gene Name
EMB1467
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
81,525 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.
NCBI/Uniprot Data
NCBI Accession #
NP_568550.1
NCBI GI #
18421656
NCBI GenBank Nucleotide #
NM_123110.2
NCBI GeneID
833729
NCBI Official Full Name
NADH-ubiquinone dehydrogenase
NCBI Official Symbol
EMB1467
NCBI Official Synonym Symbols
CI76; embryo defective 1467; MPA22.5; MPA22_5
NCBI Protein Information
NADH-ubiquinone dehydrogenase
NCBI Summary
Encodes a subunit of the 400 kDa subcomplex of the mitochondrial NADH dehydrogenase (complex I). The protein has been isolated in the male gametophyte.
UniProt Gene Name
EMB1467
UniProt Protein Name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
UniProt Synonym Protein Names
Protein EMBRYO DEFECTIVE 1467
UniProt Primary Accession #
Q9FGI6
UniProt Secondary Accession #
Q940B1
UniProt Related Accession #
Q9FGI6
UniProt Comments
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone . This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized .
For research use only, not for clinical use.