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ATP5D Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 1 - ATP5D Antibody (C-term) AP20890c
    Western blot analysis of lysates from A549, HepG2, Jurkat cell line, mouse brain tissue lysate, rat PC-12 cell line (from left to right), using ATP5D Antibody (C-term)(Cat. #AP20890c). AP20890c was diluted at 1:1000 at each lane. A goat anti-rabbit IgG H&L(HRP) at 1:10000 dilution was used as the secondary antibody. Lysates at 20ug per lane.
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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 P30049
Reactivity Human, Rat, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 17490 Da
Additional Information
Gene ID 513
Other Names ATP synthase subunit delta, mitochondrial, F-ATPase delta subunit, ATP5D
Target/Specificity This ATP5D antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 156-188 amino acids from the C-terminal region of human ATP5D.
Dilution WB~~1:1000-1:4000
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.
PrecautionsATP5D Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name ATP5F1D (HGNC:837)
Function Subunit delta, 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 (Probable) (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). With the central stalk subunit gamma, is essential for the biogenesis of F(1) catalytic part of the ATP synthase complex namely in the formation of F1 assembly intermediate (PubMed:29499186).
Cellular Location Mitochondrion. Mitochondrion inner membrane.
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 turnover 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.

REFERENCES

Jordan E.M.,et al.Biochim. Biophys. Acta 1130:123-126(1992).
Halleck A.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Grimwood J.,et al.Nature 428:529-535(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Hochstrasser D.F.,et al.Electrophoresis 13:992-1001(1992).

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