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Immunohistochemistry analysis of paraffin-embedded human pancreas tissue using ATP5G2 antibody.
Immunohistochemistry analysis of paraffin-embedded human pancreas tissue using ATP5G2 antibody.
Immunohistochemistry analysis of paraffin-embedded human pancreas tissue using ATP5G2 antibody.

ATP5G2 Antibody

Research Use Only
CSB-PA697579
Cusabio
ApplicationsELISA, ImmunoHistoChemistry
Product group Antibodies
ReactivityHuman
TargetATP5MC2
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Overview

  • Supplier
    Cusabio
  • Product Name
    ATP5G2 Antibody
  • Delivery Days Customer
    20
  • Applications
    ELISA, ImmunoHistoChemistry
  • Certification
    Research Use Only
  • Clonality
    Polyclonal
  • Conjugate
    Unconjugated
  • Formulation
    Liquid
  • Gene ID517
  • Target name
    ATP5MC2
  • Target description
    ATP synthase membrane subunit c locus 2
  • Target synonyms
    ATP synthase c subunit; ATP synthase F(0) complex subunit C2, mitochondrial; ATP synthase lipid-binding protein, mitochondrial; ATP synthase proteolipid P2; ATP synthase proton-transporting mitochondrial F(0) complex subunit C2; ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C2 (subunit 9); ATP synthase, H+ transporting, mitochondrial Fo complex subunit C2 (subunit 9); ATP5A; ATP5G2; ATPase protein 9; ATPase subunit C; dicyclohexylcarbodiimide (DCCD)-reactive proteolipid subunit
  • Host
    Rabbit
  • Isotype
    IgG
  • Protein IDQ06055
  • Protein Name
    ATP synthase F(0) complex subunit C2, mitochondrial
  • Scientific Description
    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. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. HAMAP-Rule MF_01396 Dyer M.R., Biochem. J. 293:51-64(1993). Higuti T., Biochim. Biophys. Acta 1173:87-90(1993). Farrell L.B., Biochem. Biophys. Res. Commun. 144:1257-1264(1987).
  • Reactivity
    Human
  • Storage Instruction
    -20°C or -80°C
  • UNSPSC
    12352203