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NDUA4 Antibody (C-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 14 - NDUA4 Antibody (C-term) AP20519b
    Immunohistochemical analysis of paraffin-embedded H. kidney section using NDUA4 Antibody (C-term)(Cat#AP20519B). AP20519B was diluted at 1:25 dilution. A undiluted biotinylated goat polyvalent antibody was used as the secondary, followed by DAB staining.
  • 3 - NDUA4 Antibody (C-term) AP20519b
    Fluorescent image of Hela cells stained with NDUA4 Antibody (C-term)(Cat#AP20519B). AP20519B was diluted at 1:25 dilution. An Alexa Fluor 488-conjugated goat anti-rabbit lgG at 1:400 dilution was used as the secondary antibody (green). DAPI was used to stain the cell nuclear (blue). Cytoplasmic actin was counterstained with Alexa Fluor® 555 conjugated with Phalloidin (red).
  • 1 - NDUA4 Antibody (C-term) AP20519b
    NDUA4 Antibody (C-term) (Cat. #AP20519b) western blot analysis in SW480,Hela cell line lysates (35ug/lane).This demonstrates the NDUA4 antibody detected the NDUA4 protein (arrow).
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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, IF, IHC-P, E
Primary Accession O00483
Reactivity Human, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 9370 Da
Antigen Region 56-80 aa
Additional Information
Gene ID 4697
Other Names Cytochrome c oxidase subunit NDUFA4, Complex I-MLRQ, CI-MLRQ, NADH-ubiquinone oxidoreductase MLRQ subunit, NDUFA4
Target/Specificity This NDUA4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 56-80 amino acids from the C-terminal region of human NDUA4.
Dilution WB~~1:1000
IF~~1:25
IHC-P~~1:100~500
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.
PrecautionsNDUA4 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name NDUFA4
Function Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (PubMed:22902835). NDUFA4 is required for complex IV maintenance (PubMed:22902835).
Cellular Location Mitochondrion inner membrane; Single-pass membrane protein
Research Areas

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

BACKGROUND

Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

REFERENCES

Kim J.W., et al. Biochem. Mol. Biol. Int. 43:669-675(1997).
Kanagarajah D., et al. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
Ebert L., et al. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
Halleck A., et al. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Scherer S.W., et al. Science 300:767-772(2003).

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