Rabbit Polyclonal GPX7 Antibody

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     All lanes : Anti-GPX7 Antibody (Center) at 1:2000 dilution Lane 1: Hela whole cell lysate Lane 2: THP-1 whole cell lysate Lane 3: RPMI 8226 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 : 21 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Immunofluorescent analysis of 4% paraformaldehyde-fixed,  0. 1% Triton X-100 permeabilized U-2OS cells labeling GPX7 with P34538 at 1/25 dilution,  followed by Dylight® 488-conjugated goat anti-Rabbit IgG secondary antibody at 1/200 dilution (green).  Immunofluorescence image showing cytoplasm staining on U-2OS cell line. Cytoplasmic actin is detected with Dylight® 554 Phalloidin at 1/500 dilution (red). The nuclear counter stain is DAPI (blue).    

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     Overlay histogram showing U-2 OS cells stained with P34538(green line).  The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min.  The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the antibody (P34538,  1:25 dilution) for 60 min at 37ºC.  The secondary antibody used was Goat-Anti-Rabbit IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed(OE188374) at 1/200 dilution for 40 min at 37ºC.  Isotype control antibody (blue line) was rabbit IgG1 (1μg/1x10^6 cells) used under the same conditions.  Acquisition of >10, 000 events was performed.    

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     Immunohistochemical analysis of paraffin-embedded human liver tissue using P34538 performed on the Leica® BOND RXm. Tissue was fixed with formaldehyde at room temperature; antigen retrieval was by heat mediation with a EDTA buffer (pH9. 0).  Samples were incubated with primary antibody(1:1000) for 1 hours at room temperature.  A undiluted biotinylated CRF Anti-Polyvalent HRP Polymer antibody was used as the secondary antibody.    

**Background of GPX7 Antibody**

Glutathione peroxidase 7 (GPX7) is a member of the glutathione peroxidase family, which plays a critical role in cellular antioxidant defense by catalyzing the reduction of hydrogen peroxide and lipid hydroperoxides. Unlike other GPX isoforms (e.g., GPX1-4), GPX7 lacks a selenocysteine residue, relying instead on cysteine for its catalytic activity. It is primarily localized in the endoplasmic reticulum (ER), where it assists in maintaining redox homeostasis and preventing oxidative damage during protein folding.

GPX7 has garnered attention for its dual role in cancer biology, acting as both a tumor suppressor and a context-dependent oncogenic factor. Dysregulation of GPX7 expression is linked to various cancers, neurodegenerative disorders, and metabolic diseases. For instance, its downregulation is associated with poor prognosis in colorectal and breast cancers, while overexpression may promote tumorigenesis in specific contexts.

Antibodies targeting GPX7 are essential tools for studying its expression, localization, and functional mechanisms. They enable techniques such as Western blotting, immunohistochemistry, and immunofluorescence, aiding in the exploration of GPX7's role in ER stress responses, redox signaling, and disease pathogenesis. However, challenges remain in ensuring antibody specificity due to structural similarities within the GPX family. Recent advances in monoclonal antibody development have improved detection accuracy, supporting deeper insights into GPX7's therapeutic potential as a biomarker or drug target.