抗PDI (RL77)抗体 | Anti-PDI (RL77) Antibody

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	Western Blot: PDI Antibody (RL77) [NB600-1164] - Analysis of 25 ug of HepG2 (Lane 1), Hela (Lane 2) and NIH-3T3 (Lane 3) cell lysates.
	Immunocytochemistry/Immunofluorescence: PDI Antibody (RL77) [NB600-1164] - Analysis of PDI using anti-PDI monoclonal antibody shows staining in A549 Cells.
	Immunohistochemistry-Paraffin: PDI Antibody (RL77) [NB600-1164] - Both normal and cancer biopsies of deparaffinized Human colon carcinoma tissues.
	Flow Cytometry: PDI Antibody (RL77) [NB600-1164] - Analysis of 3T3 cells compared to an isotype control (blue).
	Immunocytochemistry/Immunofluorescence: PDI Antibody (RL77) [NB600-1164] - Staining of rat epithelial cells.
	Immunocytochemistry/Immunofluorescence: PDI Antibody (RL77) [NB600-1164] - Analysis of NS-1 Cells.
	Immunocytochemistry/Immunofluorescence: PDI Antibody (RL77) [NB600-1164] - Analysis shows staining in HMVEC Cells.
	Immunohistochemistry-Paraffin: PDI Antibody (RL77) [NB600-1164] - Normal deparaffinized Human tonsil tissue tissues.
	Immunohistochemistry-Paraffin: PDI Antibody (RL77) [NB600-1164] - Both normal and cancer biopsies of deparaffinized Human liver tissues.
	Flow Cytometry: PDI Antibody (RL77) [NB600-1164] - Analysis of K562 cells compared to an isotype control (blue).
	Flow Cytometry: PDI Antibody (RL77) [NB600-1164] - Analysis of Hela cells compared to an isotype control (blue).

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Background

The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

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