Atp5h (NM_027862) Mouse Recombinant Protein

Specifications

Product Data
Species	Mouse
Expression Host	HEK293T
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) >MR201260 protein sequence Red=Cloning site Green=Tags(s) MAGRKLALKTIDWVSFVEVMPQNQKAIGNALKSWNETFHARLASLSEKPPAIDWAYYRANVAKPGLVDDF EKKYNALKIPVPEDKYTALVDQEEKEDVKSCAEFVSGSQLRIQEYEKQLEKMRNIIPFDQMTIDDLNEIF PETKLDKKKYPYWPHQPIENL TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-MYC/DDK
Predicted MW	18.7 kDa
Concentration	>0.05 µg/µL as determined by microplate BCA method
Purity	> 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer	25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
Note	For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
Storage	Store at -80°C after receiving vials.
Stability	Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Reference Data
RefSeq	NP_082138
Locus ID	71679
UniProt ID	Q9DCX2
Refseq Size	574
Cytogenetics	11 E2
Refseq ORF	486
Synonyms	0610009D10Rik
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. 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.[UniProtKB/Swiss-Prot Function]

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