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GAPDH Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - GAPDH Antibody AP50864
    Western blot analysis of lysate from Hela cell line,using GAPDH Antibody(AP50864). AP50864 was diluted at 1:500. A goat anti-rabbit IgG H&L(HRP) at 1:5000 dilution was used as the secondary antibody.Lysate at 35ug.
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Product info
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
Primary Accession P04406
Reactivity Human, Mouse, Rat, Rabbit
Host Rabbit
Clonality Polyclonal
Calculated MW 37; [uniprot]36,32; [EPI]36; [CST]37; KDa
Additional info
Gene ID 2597
Other Names Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, 2699-, GAPDH, GAPD
Dilution WB~~ 1:500
Format0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glyce
StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Protein Information
Name GAPDH
Synonyms GAPD
Function Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D- glyceroyl phosphate. Component of the GAIT (gamma interferon- activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.
Cellular Location Cytoplasm, cytosol. Nucleus. Cytoplasm, perinuclear region. Membrane. Cytoplasm, cytoskeleton. Note=Translocates to the nucleus following S- nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnuclear and Perinuclear regions.
Research Areas

BACKGROUND

Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D- glyceroyl phosphate. Component of the GAIT (gamma interferon- activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.

REFERENCES

Hanauer A.,et al.EMBO J. 3:2627-2633(1984).
Arcari P.,et al.Nucleic Acids Res. 12:9179-9189(1984).
Tso J.Y.,et al.Nucleic Acids Res. 13:2485-2502(1985).
Tokunaga K.,et al.Cancer Res. 47:5616-5619(1987).
Allen R.W.,et al.J. Biol. Chem. 262:649-653(1987).

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