Product Details
| Alternative Name: | Tra1, Tumor rejection antigen 1, Hsp90B1, Gp96, Heat shock protein 90 kDa beta member 1, Endoplasmin |
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| MW: | ~94kDa |
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| Source: | Produced in Sf21 insect cells. Produced in a baculovirus expression system. |
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| UniProt ID: | P41148 |
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| Formulation: | Liquid. In 20mM MOPS, pH 7.5, containing 0.5mM EDTA. |
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| Purity: | ≥90% (SDS-PAGE; Western blot) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Applications: | WB
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| Application Notes: | Western blot control. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | Grp94 (Glucose-regulated protein 94) is an abundant resident endoplasmic reticulum (ER) lumenal stress protein, which together with cytosolic Hsp90 belongs to the Hsp90 family of molecular chaperones. Grp94 expression is upregulated by stress conditions such as glucose starvation and heat shock, which promote protein misfolding or unfolding. In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. |
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| Regulatory Status: | RUO - Research Use Only |
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Western Blot analysis: 100 ng of Grp94 (canine), (recombinant) probed with Prod. No. ADI-SPA-850.
SDS-PAGE analysis: Lane 1: MW marker, Lane 2: 0.5µg; Lane 3: 1µg; Lane 4: 2µg; Lane 5: 5µg of Grp94 (canine), (recombinant) detected by Coomassie Stain
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Product Literature References
Experimental Anti-Inflammatory Drug Semapimod Inhibits TLR Signaling by Targeting the TLR Chaperone gp96: J. Wang, et al.; J. Immunol.
196, 5130 (2016),
Abstract;
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