Atp5a1 (NM_007505) Mouse Tagged ORF Clone Lentiviral Particle

SKU MR208769L1V

Lenti ORF particles, Atp5a1 (Myc-DDK-tagged) - Mouse ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 (Atp5a1), nuclear gene encoding mitochondrial protein, 200ul, >10^7 TU/mL

Product Data

• Type: Mouse Tagged ORF Clone Lentiviral Particle
• Tag: Myc-DDK
• Target Symbol: Atp5a1
• Synonyms: AI035633; AL022851; AL023067; Atpm; D18Ertd206e; Mom2
• Vector: pLenti-C-Myc-DDK
• Mammalian Cell Selection: None
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(MR208769).
• ACCN: NM_007505
• ORF Size: 1659 bp
• OTI Disclaimer: The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info
• OTI Annotation: This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene.
• Shipping: Dry Ice

Reference Data

• RefSeq: NM_007505.2, NP_031531.1
• RefSeq Size: 2443 bp
• RefSeq ORF: 1662 bp
• Locus ID: 11946
• UniProt ID: Q03265
• Cytogenetics: 18 52.38 cM
• Summary: Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).[UniProtKB/Swiss-Prot Function]