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Home Antibody All anti-HSP90B1 antibodies

Anti-HSP90B1 Antibody 9G10

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Specifications Citations Related Products Product Documents
SKU Description Amount Price Availability*  
TA326419
  • Mouse monoclonal GRP94 Antibody
200µg $325 3-7 Days
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WB(1)
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Also for HSP90B1 (NM_003299)
cDNA Clone shRNA/siRNA Lysate Protein Antibody

OriGene Data

ImmunogenPurified Grp94 isolated from chicken oviducts
Clone Name9G10 IsotypeIgG2a
Species ReactivityHuman, Mouse, Rat, Bovine, Canine, Chicken, Guinea pig, Hamster, Horse, Monkey, Pig, Rabbit, Sheep, Xenopus Concentration1mg/mL
Guaranteed Application *WB Suggested Dilutions0.5ug/ml was sufficient for detection of Grp94 in 20ug of HeLa lysate.
BufferPBS pH7.2, 50% glycerol, 0.09% sodium azide
Purification Protein G Purified
Note Detects a 98kDa protein corresponding to the molecular mass of Grp94 on SDS PAGE immunoblots. Does not detect human Hsp90, Grp74, or GrpE from E.coli.

Reference Data

Target NameHomo sapiens heat shock protein 90kDa beta (Grp94), member 1 (HSP90B1)
Alternative NameECGP; GP96; GRP94; HEL-S-125m; HEL35; TRA1
Database LinkNP_003290
FunctionGrp94 (glucose regulated protein 94, gp96) 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 . Grp94 also plays a role in antigen presentation by accessing the endogenous pathway and eliciting specific CTL responses to chaperone bound peptides via MHC class I pathway Grp94 is a member of the Hsp90 family of stress proteins and shares sequence homolgy with its cytosolic equivalent, Hsp90 . Both Hsp90 and Grp94 are calcium binding proteins . 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 hydrolyisis activity . 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. . Grp94 contains a carboxy terminal KDEL (Lys-Asp-Glu-Leu) sequence which is believed to aid in its retention in the ER .
Related Pathway

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WB Image
Western blot analysis of Grp94 using Hela cell lysate at 1:1000 dilution of the antibody

 

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