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Anti-ATP5A1 antibody

SKU Product Brand Unit Availability Price Quantity  
AB-06-0415
Anti-ATP5A1 antibody
Erpan Tech In stock

Specifications        

Product Cat#: AB-06-0415
Product type: Primary antibody
Antigen: ATP5A1
Immunogen: Recombinant protein
Species immunized: Rabbit
Isotype: IgG
Applications: Western Blot (1:1000-1:5000); Immunocytochemistry/Immunofluorescence (1:100-1:500); Immunohistochemistry (1:50-1:200); Flow Cytometry (1:40-1:100)
Reactivity: Mouse, Rat and Human
Clonality (clone number): Monoclonal, JM110-04
Form: Liquid
Buffer: Tris-HCl buffer (pH7.4), 1% BSA, 40% glycerol, 0.05% NaN3.
Concentration: 1 mg/ml
Purity: Protein A/G affinity purified
Storage: Aliquot and freeze at -20℃. Avoid multiple freeze/thaw cycles.
Alternative names: ATP synthase alpha chain, mitochondrial antibody
ATP synthase subunit alpha antibody
ATP synthase subunit alpha mitochondrial antibody
ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle antibody
ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, 1 antibody
ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 1, cardiac muscle antibody
ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 2, non-cardiac muscle-like 2 antibody
ATP sythase (F1 ATPase) alpha subunit antibody
ATP5A antibody
Atp5a1 antibody
ATP5AL2 antibody
ATPA_HUMAN antibody
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Mitochondrial antibody
Mitochondrial ATP synthetase antibody
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Modifier of Min 2 mouse homolog antibody
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Target information

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 synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 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 (PubMed:30146159).

Provider

Erpantech Laboratory

download

MSDS-AB-06-0415.pdf (206 downloads )