ATP synthase subunit delta', mitochondrial, Recombinant Protein

Full Product Name

Recombinant Pisum sativum ATP synthase subunit delta', mitochondrial

Purity

Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)

Sequence

STDVATPATN SSFVEAWRKV SPNIDPPKTP LEFLKTRPPV PSTIPTKLTV NFVLPYSSQL AAKEVDSVII PATTGEMGVL PGHVATIAEL KPGVLTVQEG TDTTKYFVSS GFRFIHANSV ADIIAVEAVP VNQLDRDLVQ KGLQEFTQKL NSATTDLEKR EAQIGIDVDS ALNSALTG

Sequence Positions

20-197, Full length protein

Format

Lyophilized or liquid (Format to be determined during the manufacturing process)

Host

E Coli or Yeast or Baculovirus or Mammalian Cell

Molecular Weight

21,274 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 synthase

NCBI Accession #

Q41000.1

NCBI GI #

2493047

NCBI Official Full Name

ATP synthase subunit delta', mitochondrial

UniProt Protein Name

ATP synthase subunit delta', mitochondrial

UniProt Synonym Protein Names

F-ATPase delta' subunit

UniProt Primary Accession #

Q41000

UniProt Comments

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.