Cusabio Human Recombinants
Recombinant Human ATP synthase subunit O, mitochondrial (ATP5O) | CSB-EP002379HU
- SKU:
- CSB-EP002379HU
- Availability:
- 3 - 7 Working Days
Description
Recombinant Human ATP synthase subunit O, mitochondrial (ATP5O) | CSB-EP002379HU | Cusabio
Alternative Name(s): Oligomycin sensitivity conferral protein ;OSCP
Gene Names: ATP5O
Research Areas: Metabolism
Organism: Homo sapiens (Human)
AA Sequence: FAKLVRPPVQVYGIEGRYATALYSAASKQNKLEQVEKELLRVAQILKEPKVAASVLNPYVKRSIKVKSLNDITAKERFSPLTTNLINLLAENGRLSNTQGVVSAFSTMMSVHRGEVPCTVTSASPLEEATLSELKTVLKSFLSQGQVLKLEAKTDPSILGGMIVRIGEKYVDMSVKTKIQKLGRAMREIV
Source: E.coli
Tag Info: N-terminal GST-tagged
Expression Region: 24-213aa
Sequence Info: Full Length of Mature Protein
MW: 47.9 kDa
Purity: Greater than 90% as determined by SDS-PAGE.
Relevance: Mitochondrial mbrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the mbrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extrambraneous catalytic core and F0 - containing the mbrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elents.
Reference: "Complete sequencing and characterization of 21,243 full-length human cDNAs."Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004)
Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20?/-80?. The shelf life of lyophilized form is 12 months at -20?/-80?.
Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.
Function: 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Involvement in disease:
Subcellular Location: Mitochondrion, Mitochondrion inner membrane
Protein Families: ATPase delta chain family
Tissue Specificity:
Paythway: OxidativePhosphorylation
Form: Liquid or Lyophilized powder
Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20?/-80?. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Uniprot ID: P48047
HGNC Database Link: HGNC
UniGene Database Link: UniGene
KEGG Database Link: KEGG
STRING Database Link: STRING
OMIM Database Link: OMIM