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  2. HSP (Heat shock proteins)
  3. GRP94 Monoclonal Antibody (Clone 9G10)
  • GRP94 Monoclonal Antibody (Clone 9G10)
GRP94 Monoclonal Antibody (Clone 9G10)的可视化放大

GRP94 Monoclonal Antibody (Clone 9G10)

For immunochemical detection of GRP94

原价
￥2037-6137
价格
￥ 1630-4910
GRP94 Monoclonal Antibody (Clone 9G10)的二维码

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  • 库存: 现货
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  • 货号: ajcx26416
  • CAS: N/A
  • 别名:
  • 分子式: N/A
  • 分子量: 98
  • 纯度: >98%
  • 溶解度: N/A
  • 储存: -20°C
  • 库存: 现货

Background


Glucose regulated protein 94 (GRP94) is a constitutively expressed endoplasmic reticulum (ER) lumenal protein that is up-regulated in response to cellular stress such as heat shock, oxidative stress or glucose depletion. GRP94 is thought to play a role in protein translocation to the ER, in their subsequent folding and assembly, and in regulating protein secretion.1 GRP94 also plays a role in antigen presentation by accessing the endogenous pathway and eliciting specific cytotoxic T lymphocyte (CTL) responses to chaperone bound peptides via the major histocompatibility complex (MHC) class I pathway.2 GRP94 is a member of the Hsp90 family of stress proteins and shares sequence homology with its cytosolic equivalent, Hsp90.3 Both Hsp90 and GRP94 are calcium binding proteins.4 Despite sharing 50% sequence homology over its N domains and complete conservation in its ligand binding domains with Hsp90, GRP94, and Hsp90 differ in their interactions with regulatory ligands as GRP94 has weak ATP binding and hydrolysis activity.5 GRP94 exists as a homodimer and the two subunits interact at two distinct intermolecular sites, C-terminal dimerization domains and the N-terminal interacts with the middle domain of opposing subunits.6 GRP94 contains a carboxy terminal KDEL (Lys-Asp-Glu-Leu) sequence which is believed to aid in its retention in the ER.7


1.Ruddon, R.W., and Bedows, E.Assisted protein foldingThe Journal of Biological Chemisty272(6)3125-3128(1997) 2.Srivastava, P.K., Udono, H., Blachere, N.E., et al.Heat shock protein transfer peptides during antigen processing and CTL primingImmunogenetics39(2)93-98(1994) 3.Mazzarella, R.A., and Green, M.ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)The Journal of Biological Chemisty262(18)8875-8883(1987) 4.Kang, H.S., and Welch, W.J.Characterization and purification of the 94-kDa glucose-regulated proteinThe Journal of Biological Chemisty266(9)5643-5649(1991) 5.Soldano, K.L., Jivan, A., Nicchitta, C.V., et al.Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulationThe Journal of Biological Chemisty278(48)48330-48338(2003) 6.Chu, F., Maynard, J.C., Chiosis, G., et al.Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94Protein Science151260-1269(2006) 7.Peter, F., Van, P.N., and S?ling, H.D.Different sorting of Lys-Asp-Glu-Leu proteins in rat liverThe Journal of Biological Chemisty267(15)10631-10637(1992)

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