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>   首页   >   产品   >   一抗   >   代谢   >   ATP5E Antibody (C-Term)   

ATP5E Antibody (C-Term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - ATP5E Antibody (C-Term) AP21888b
    All lanes : Anti-ATP5E Antibody (C-Term) at 1:2000 dilution Lane 1: human heart lysate Lane 2: human skeletal muscle lysate Lane 3: Hela whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 6 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P56381
Reactivity Human
Host Rabbit
Clonality polyclonal
Isotype Rabbit IgG
Calculated MW 5780 Da
Additional Information
Gene ID 514
Other Names ATP synthase subunit epsilon, mitochondrial, ATPase subunit epsilon, ATP5E
Target/Specificity This ATP5E antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 21-51 amino acids from human ATP5E.
Dilution WB~~1:2000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsATP5E Antibody (C-Term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name ATP5F1E (HGNC:838)
Function Subunit epsilon, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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 (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). 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 (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). May be essential for the assembly of F(1) and may play an important role in the incorporation of the hydrophobic subunit c into the F(1)-c oligomer rotor of the mitochondrial ATP synthase complex (PubMed:20026007).
Cellular Location Mitochondrion. Mitochondrion inner membrane.
Tissue Location Ubiquitous.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

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(1) domain and of the central stalk which is part of the complex rotary element. 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 (By similarity).

REFERENCES

Tu Q.,et al.Biochem. J. 347:17-21(2000).
Hu R.-M.,et al.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Deloukas P.,et al.Nature 414:865-871(2001).

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