Rabbit Polyclonal gp78 antibody. Suitable for ICC/IF and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human AMFR aa 500 to C-terminus.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: PBS, 40% Glycerol (glycerin, glycerine)
ICC/IF | |
---|---|
Human | Tested |
Mouse | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 0.25000-2.00000 µg/mL | Notes Fixation/Permeabilization: PFA/Triton X-100. |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info - | Notes - |
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E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins, such as CD3D, CYP3A4, CFTR, INSIG1, SOAT2/ACAT2 and APOB for proteasomal degradation (PubMed:10456327, PubMed:11724934, PubMed:12670940, PubMed:19103148, PubMed:24424410, PubMed:28604676). Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD) (PubMed:10456327, PubMed:11724934, PubMed:19103148, PubMed:24424410). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG1 complex at the ER membrane (PubMed:16168377, PubMed:22143767). In addition, interaction of AMFR with AUP1 facilitates interaction of AMFR with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase RNF139, leading to sterol-induced HMGCR ubiquitination (PubMed:23223569). The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction (PubMed:16168377, PubMed:22143767, PubMed:23223569). In addition to ubiquitination on lysine residues, catalyzes ubiquitination on cysteine residues: together with INSIG1, mediates polyubiquitination of SOAT2/ACAT2 at 'Cys-277', leading to its degradation when the lipid levels are low (PubMed:28604676). Catalyzes ubiquitination and subsequent degradation of INSIG1 when cells are depleted of sterols (PubMed:17043353). Mediates polyubiquitination of INSIG2 at 'Cys-215' in some tissues, leading to its degradation (PubMed:31953408). Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex (PubMed:21636303). Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation (PubMed:21636303). Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor (PubMed:10456327). In association with LMBR1L and UBAC2, negatively regulates the canonical Wnt signaling pathway in the lymphocytes by promoting the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (PubMed:31073040). Regulates NF-kappa-B and MAPK signaling pathways by mediating 'Lys-27'-linked polyubiquitination of TAB3 and promoting subsequent TAK1/MAP3K7 activation (PubMed:36593296). Required for proper lipid homeostasis (PubMed:37119330).
RNF45, AMFR, E3 ubiquitin-protein ligase AMFR, Autocrine motility factor receptor, RING finger protein 45, gp78, AMF receptor
Rabbit Polyclonal gp78 antibody. Suitable for ICC/IF and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human AMFR aa 500 to C-terminus.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: PBS, 40% Glycerol (glycerin, glycerine)
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Gp78 also known as AMFR (Autocrine Motility Factor Receptor) functions as an E3 ubiquitin ligase within the endoplasmic reticulum (ER). This protein exhibits a mass of around 78 kDa. You can find gp78 expressed in several tissues but with strong presence in the liver. It is integral to the ER-associated degradation (ERAD) pathway where it tags misfolded proteins with ubiquitin for subsequent degradation by the proteasome maintaining protein quality control within cells.
Gp78 acts as a regulator of protein degradation by forming a complex with other proteins like Ubc7 and Derlin-1. It ensures the balance between protein synthesis and degradation. Gp78 aids in dislocating misfolded proteins from the ER lumen into the cytosol facilitating their destruction. Through its E3 ligase activity gp78 helps control cellular protein levels reducing the stress on cells when protein folding is imperfect.
Gp78 plays a role in the ubiquitin-proteasome pathway and the ERAD pathway. These pathways manage protein turnover and ER stress response. In these processes gp78 interacts with proteins such as VCP/p97 which assists in extracting the ubiquitinated proteins from the ER membrane. This cooperation highlights gp78’s involvement in maintaining cellular homeostasis helping cells adapt to changes in the ER environment.
Gp78 shows a connection to cancer and neurodegenerative diseases. Overexpression of gp78 has been linked to metastasis in cancer where it may influence the regulation of cell motility and invasion capabilities. Additionally alterations in the activity of gp78 have implications in neurodegenerative disorders like Parkinson's disease where misfolded protein accumulation is problematic. In these contexts gp78 interacts with proteins such as Parkin an E3 ligase also involved in protein degradation further emphasizing its role in disease-related protein quality control.
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A549 cells stained for gp78 (green) using ab222051 (4 μg/ml) in immunocytochemistry/ immunofluorescence.
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