Home Antibody All anti-HSP90B1 antibodies
Anti-HSP90B1 Antibody 9G10
Write Review & Get Rewarded
Write a review and get rewarded!
Review this antibody and earn an OriGene coupon or Amazon giftcard
Follow these easy steps to reward yourself:
- Sign in to your account, or register for a new account;
- Write a review;
- Receive a coupon or giftcard once your review is accepted.
Click the button to start writing a review
Also for HSP90B1 (NM_003299)
|Purified Grp94 isolated from chicken oviducts|
|Human, Mouse, Rat, Bovine, Canine, Chicken, Guinea pig, Hamster, Horse, Monkey, Pig, Rabbit, Sheep, Xenopus
||0.5ug/ml was sufficient for detection of Grp94 in 20ug of HeLa lysate.
|PBS pH7.2, 50% glycerol, 0.09% sodium azide |
|Protein G Purified
|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.
|Homo sapiens heat shock protein 90kDa beta (Grp94), member 1 (HSP90B1)|
|ECGP; GP96; GRP94; HEL-S-125m; HEL35; TRA1|
Entrez Gene 7184 Human
Entrez Gene 22027 Mouse
Entrez Gene 362862 Rat
Entrez Gene 708759 Monkey
|Grp94 (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 .|
|Druggable Genome NOD-like receptor signaling pathwayPathways in cancerProstate cancer|
* Availability is in business days
* OriGene provides validated application data and protocol, with money back guarantee.
Western blot analysis of Grp94 using Hela cell lysate at 1:1000 dilution of the antibody