|Application ||WB, IHC-P, E|
|Predicted||Human, Mouse, Rat, Rabbit, Hamster, Monkey, Pig, Sheep, Bovine, Horse|
|Calculated MW||59751 Da|
|Dilution||ELISA (1:128000), IHC-P (5 µg/ml), WB (0.01 - 0.03 µg/ml)|
|Other Names||ATP5A1, ATP5AL2, ATP5A, HATP1, Mitochondrial ATP synthase, MOM2, ORM, OMR, ATPM|
|Target/Specificity||Human ATP5A1 / ATP Synthase Alpha. This antibody is expected to recognize all reported isoforms (NP_004037.1; NP_001244263.1; NP_001001935.1).|
|Reconstitution & Storage||Immunoaffinity purified|
|Precautions||Anti-ATP5A1 / ATP Synthase Alpha Antibody (aa83-94) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||ATP5A, ATP5AL2, ATPM|
|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. 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).|
|Cellular Location||Mitochondrion inner membrane. Cell membrane; Peripheral membrane protein; Extracellular side. Note=Colocalizes with HRG on the cell surface of T-cells|
|Tissue Location||Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord.|
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