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rabbit polyclonal anti grp94 antibody  (Proteintech)


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    Structured Review

    Proteintech rabbit polyclonal anti grp94 antibody
    Mechanism of action of IRE1/XBP1s activators on enhancing GABA A R variant proteostasis. Certain GABA A R variants misfold in the ER and undergo excessive ER-associated degradation (ERAD), leading to their trafficking deficiency to the plasma membrane. IRE1/XBP1s activators enhance the ER folding capacity to promote the folding of a variant by increasing the interaction between the variant and BiP, a pro-folding chaperone, and further promote the assembly into pentameric receptors in the ER membrane. In addition, such IRE1/XBP1s activators inhibit the ERAD of the variant by decreasing the interaction between the variant and <t>Grp94,</t> Hrd1-Sel1L, and VCP, known ERAD factors for GABA A Rs. Consequently, IRE1/XBP1s activators enhance the anterograde trafficking of the variant to the plasma membrane by increasing the interaction between the variant and LMAN1. The receptor variant is also stabilized after reaching the plasma membrane.
    Rabbit Polyclonal Anti Grp94 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 116 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+grp94+antibody/pmc12679549-191-1-10?v=Proteintech
    Average 95 stars, based on 116 article reviews
    rabbit polyclonal anti grp94 antibody - by Bioz Stars, 2026-08
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    1) Product Images from "Improving Proteostasis of Trafficking-Deficient GABA A Receptor Variants by Activating IRE1"

    Article Title: Improving Proteostasis of Trafficking-Deficient GABA A Receptor Variants by Activating IRE1

    Journal: ACS Chemical Neuroscience

    doi: 10.1021/acschemneuro.5c00227

    Mechanism of action of IRE1/XBP1s activators on enhancing GABA A R variant proteostasis. Certain GABA A R variants misfold in the ER and undergo excessive ER-associated degradation (ERAD), leading to their trafficking deficiency to the plasma membrane. IRE1/XBP1s activators enhance the ER folding capacity to promote the folding of a variant by increasing the interaction between the variant and BiP, a pro-folding chaperone, and further promote the assembly into pentameric receptors in the ER membrane. In addition, such IRE1/XBP1s activators inhibit the ERAD of the variant by decreasing the interaction between the variant and Grp94, Hrd1-Sel1L, and VCP, known ERAD factors for GABA A Rs. Consequently, IRE1/XBP1s activators enhance the anterograde trafficking of the variant to the plasma membrane by increasing the interaction between the variant and LMAN1. The receptor variant is also stabilized after reaching the plasma membrane.
    Figure Legend Snippet: Mechanism of action of IRE1/XBP1s activators on enhancing GABA A R variant proteostasis. Certain GABA A R variants misfold in the ER and undergo excessive ER-associated degradation (ERAD), leading to their trafficking deficiency to the plasma membrane. IRE1/XBP1s activators enhance the ER folding capacity to promote the folding of a variant by increasing the interaction between the variant and BiP, a pro-folding chaperone, and further promote the assembly into pentameric receptors in the ER membrane. In addition, such IRE1/XBP1s activators inhibit the ERAD of the variant by decreasing the interaction between the variant and Grp94, Hrd1-Sel1L, and VCP, known ERAD factors for GABA A Rs. Consequently, IRE1/XBP1s activators enhance the anterograde trafficking of the variant to the plasma membrane by increasing the interaction between the variant and LMAN1. The receptor variant is also stabilized after reaching the plasma membrane.

    Techniques Used: Variant Assay, Clinical Proteomics, Membrane



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    Image Search Results


    Mechanism of action of IRE1/XBP1s activators on enhancing GABA A R variant proteostasis. Certain GABA A R variants misfold in the ER and undergo excessive ER-associated degradation (ERAD), leading to their trafficking deficiency to the plasma membrane. IRE1/XBP1s activators enhance the ER folding capacity to promote the folding of a variant by increasing the interaction between the variant and BiP, a pro-folding chaperone, and further promote the assembly into pentameric receptors in the ER membrane. In addition, such IRE1/XBP1s activators inhibit the ERAD of the variant by decreasing the interaction between the variant and Grp94, Hrd1-Sel1L, and VCP, known ERAD factors for GABA A Rs. Consequently, IRE1/XBP1s activators enhance the anterograde trafficking of the variant to the plasma membrane by increasing the interaction between the variant and LMAN1. The receptor variant is also stabilized after reaching the plasma membrane.

    Journal: ACS Chemical Neuroscience

    Article Title: Improving Proteostasis of Trafficking-Deficient GABA A Receptor Variants by Activating IRE1

    doi: 10.1021/acschemneuro.5c00227

    Figure Lengend Snippet: Mechanism of action of IRE1/XBP1s activators on enhancing GABA A R variant proteostasis. Certain GABA A R variants misfold in the ER and undergo excessive ER-associated degradation (ERAD), leading to their trafficking deficiency to the plasma membrane. IRE1/XBP1s activators enhance the ER folding capacity to promote the folding of a variant by increasing the interaction between the variant and BiP, a pro-folding chaperone, and further promote the assembly into pentameric receptors in the ER membrane. In addition, such IRE1/XBP1s activators inhibit the ERAD of the variant by decreasing the interaction between the variant and Grp94, Hrd1-Sel1L, and VCP, known ERAD factors for GABA A Rs. Consequently, IRE1/XBP1s activators enhance the anterograde trafficking of the variant to the plasma membrane by increasing the interaction between the variant and LMAN1. The receptor variant is also stabilized after reaching the plasma membrane.

    Article Snippet: The rabbit polyclonal anti-Grp94 antibody (#14700-1-AP, 1:250) was obtained from Proteintech.

    Techniques: Variant Assay, Clinical Proteomics, Membrane

    Expression of the PNLIP p.S290N variant induced increased ER stress and the UPR in vitro. HEK 293T cells were transfected to express PNLIP p.S290N and WT. Samples were harvested 68 h post-transfection for immunoblotting and qPCR analysis for ER stress and the UPR markers as described in the Methods. A: Representative immunoblot images for various markers. α-tubulin served as a control. The relative protein abundance for each marker in different cell lysate fractions presented in (A) was quantified relative to WT, with the exception for the insoluble fraction where the values were expressed as relative to S290N. B: Relative BiP protein abundance. C: Relative GRP94 protein abundance. D: Relative mRNA abundance of BiP and CHOP by qPCR. E: A representative image of semi-quantitative PCR analysis of Xbp1 mRNA splicing. F: Quantification of Xbp1 mRNA splicing presented in (E). Mock, empty vector; WT, wild type. The values in quantification graphs are expressed as the mean ± S.D. of 6 or more independent experiments, and One-Way ANOVA Mixed-effects analysis by Tukey's multiple comparisons were performed.

    Journal: Journal of Lipid Research

    Article Title: Characterization of a PNLIP variant identified in Amish pediatric patients with congenital pancreatic lipase deficiency

    doi: 10.1016/j.jlr.2025.100878

    Figure Lengend Snippet: Expression of the PNLIP p.S290N variant induced increased ER stress and the UPR in vitro. HEK 293T cells were transfected to express PNLIP p.S290N and WT. Samples were harvested 68 h post-transfection for immunoblotting and qPCR analysis for ER stress and the UPR markers as described in the Methods. A: Representative immunoblot images for various markers. α-tubulin served as a control. The relative protein abundance for each marker in different cell lysate fractions presented in (A) was quantified relative to WT, with the exception for the insoluble fraction where the values were expressed as relative to S290N. B: Relative BiP protein abundance. C: Relative GRP94 protein abundance. D: Relative mRNA abundance of BiP and CHOP by qPCR. E: A representative image of semi-quantitative PCR analysis of Xbp1 mRNA splicing. F: Quantification of Xbp1 mRNA splicing presented in (E). Mock, empty vector; WT, wild type. The values in quantification graphs are expressed as the mean ± S.D. of 6 or more independent experiments, and One-Way ANOVA Mixed-effects analysis by Tukey's multiple comparisons were performed.

    Article Snippet: The following primary antibodies were used: a rabbit polyclonal antibody against human PNLIP generated in our lab (1:5,000) , a rabbit polyclonal antibody against BiP (1:1,000; Cat.: 3183, Cell Signaling), a rabbit polyclonal antibody against GRP94 (1:1,000; Cat.: 2104, Cell Signaling), and a rat monoclonal antibody against α-tubulin (1:2,000; Cat.: sc-53029, Santa Cruz Biotechnology) used as an endogenous control.

    Techniques: Expressing, Variant Assay, In Vitro, Transfection, Western Blot, Control, Quantitative Proteomics, Marker, Real-time Polymerase Chain Reaction, Plasmid Preparation

    KEY RESOURCES TABLE

    Journal: Cell reports

    Article Title: Mechanism and evolutionary origins of alanine-tail C-degron recognition by E3 ligases Pirh2 and CRL2-KLHDC10

    doi: 10.1016/j.celrep.2023.113100

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Rabbit polyclonal anti-GRP94 , Cell Signaling Technology , Cat# 2104: RRID: AB_823506.

    Techniques: Virus, Recombinant, Protease Inhibitor, Amplified Luminescent Proximity Homogenous Assay, Lysis, TA Cloning, Sequencing, Software