Bio-Connect

GRP94 antibody [N1N3]

GTX103203
GeneTex
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
TargetHSP90B1
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Overview

  • Supplier
    GeneTex
  • Product Name
    GRP94 antibody [N1N3]
  • Delivery Days Customer
    9
  • Application Supplier Note
    WB: 1:500-1:10000. ICC/IF: 1:100-1:1000. IHC-P: 1:100-1:1000. IP: 1:100-1:500. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
  • Certification
    Research Use Only
  • Clonality
    Polyclonal
  • Concentration
    0.95 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID7184
  • Target name
    HSP90B1
  • Target description
    heat shock protein 90 beta family member 1
  • Target synonyms
    ECGP, GP96, GRP94, HEL-S-125m, HEL35, TRA1, endoplasmin, 94 kDa glucose-regulated protein, endothelial cell (HBMEC) glycoprotein, epididymis luminal protein 35, epididymis secretory sperm binding protein Li 125m, heat shock protein 90 kDa beta member 1, heat shock protein 90kDa beta (Grp94), member 1, heat shock protein 90kDa beta family member 1, heat shock protein family C member 4, stress-inducible tumor rejection antigen gp96, tumor rejection antigen (gp96) 1, tumor rejection antigen 1
  • Host
    Rabbit
  • Isotype
    IgG
  • Protein IDP14625
  • Protein Name
    Endoplasmin
  • Scientific Description
    HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Arlt A, Kohlschmidt N, Hentschel A, et al. Novel insights into PORCN mutations, associated phenotypes and pathophysiological aspects. Orphanet J Rare Dis. 2022,17(1):29. doi: 10.1186/s13023-021-02068-w
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  • Lee CW, Huang CC, Chi MC, et al. Naringenin Induces ROS-Mediated ER Stress, Autophagy, and Apoptosis in Human Osteosarcoma Cell Lines. Molecules. 2022,27(2). doi: 10.3390/molecules27020373
    Read this paper
  • Gatz C, Hathazi D, Münchberg U, et al. Identification of Cellular Pathogenicity Markers for SIL1 Mutations Linked to Marinesco-Sjögren Syndrome. Front Neurol. 2019,10:562. doi: 10.3389/fneur.2019.00562
    Read this paper
  • Ramírez-Peinado S, Ignashkova TI, van Raam BJ, et al. TRAPPC13 modulates autophagy and the response to Golgi stress. J Cell Sci. 2017,130(14):2251-2265. doi: 10.1242/jcs.199521
    Read this paper
  • Plate L, Cooley CB, Chen JJ, et al. Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation. Elife. 2016,5:pii: e15550. doi: 10.7554/eLife.15550.
    Read this paper
  • Krishnan S, Chang AC, Hodges J, et al. Serotype O18 avian pathogenic and neonatal meningitis Escherichia coli strains employ similar pathogenic strategies for the onset of meningitis. Virulence. 2015,6(8):777-86. doi: 10.1080/21505594.2015.1091914
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  • Cooley CB, Ryno LM, Plate L, et al. Unfolded protein response activation reduces secretion and extracellular aggregation of amyloidogenic immunoglobulin light chain. Proc Natl Acad Sci U S A. 2014,111(36):13046-51. doi: 10.1073/pnas.1406050111
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