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AB188463

Recombinant Human GRP94 protein (Tagged-His Tag)

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(1 Publication)

Recombinant Human GRP94 protein (Tagged-His Tag) is a Human Fragment protein, in the 22 to 798 aa range, expressed in HEK 293 cells, with >90%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, ELISA, WB, Mass Spec.

View Alternative Names

GRP94, HSPC4, TRA1, HSP90B1, Endoplasmin, 94 kDa glucose-regulated protein, Heat shock protein 90 kDa beta member 1, Heat shock protein family C member 4, Tumor rejection antigen 1, gp96 homolog, GRP-94

1 Images
SDS-PAGE - Recombinant Human GRP94 protein (Tagged-His Tag) (AB188463)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human GRP94 protein (Tagged-His Tag) (AB188463)

14 % SDS-PAGE separation of Human GRP94 :
1. MW marker - 14, 21, 31, 45, 66, 97 kDa
2. Reduced and boiled sample, 2.5 μg/lane
3. Non-reduced and non-boiled sample, 2.5 μg/lane

Key facts

Purity

>90% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

SDS-PAGE, ELISA, Mass Spec, WB

applications

Biologically active

No

Accession

P14625

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in 200 µL of water

Storage buffer

Constituents: PBS, 4% Mannitol, 1% Sucrose

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"ASDDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEETAKESTAEGPKLHHHHHH","proteinLength":"Fragment","predictedMolecularWeight":"90.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":798,"aminoAcidStart":22,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P14625","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

GRP94 also known as HSP90b1 is a glycoprotein that belongs to the heat shock protein 90 family. It has a molecular mass of approximately 94 kDa. GRP94 is expressed mainly in the endoplasmic reticulum and appears in high levels in cells undergoing stress. This protein acts as a chaperone assisting in the proper folding and assembly of other proteins playing an essential role in protein homeostasis. GRP94 ensures the quality control of proteins by preventing misfolding and aggregation.
Biological function summary

GRP94 influences the stability of many secretory and cell-surface proteins. It forms part of a multi-protein complex that stabilizes client proteins and assists their proper folding. GRP94 is essential for the maturation of proteins involved in the immune response including immunoglobulins and integrins. Overexpression of GRP94 has been noted in various cancers where it supports the folding of proteins required for tumor growth and survival.

Pathways

GRP94 is an important element of the protein folding quality control mechanism within the endoplasmic reticulum. It functions in coordination with other chaperones like BiP and calnexin within the unfolded protein response (UPR) pathway. The UPR pathway is essential during stress conditions where increased protein synthesis occurs. GRP94 also contributes to calcium homeostasis and directly interacts with proteins like integrins affecting cell adhesion and motility.

GRP94 has been implicated in the progression of cancer and neurodegenerative diseases. Overexpression of GRP94 is often linked to cancer where it stabilizes oncogenic proteins necessary for cancer cell survival. In neurodegenerative disorders GRP94 shows altered expression levels which may influence the pathogenesis of diseases like Alzheimer's. The interaction between GRP94 and other proteins such as tau protein in Alzheimer's highlights its potential role in disease mechanisms.

Specifications

Form

Lyophilized

General info

Function

Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed : 18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed : 32272059).

Sequence similarities

Belongs to the heat shock protein 90 family.

Product protocols

Target data

Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed : 18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed : 32272059).
See full target information HSP90B1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Analytical and bioanalytical chemistry 408:1497-506 PubMed26715250

2015

Anti-heat shock protein autoantibody profiling in breast cancer using customized protein microarray.

Applications

Unspecified application

Species

Unspecified reactive species

Liu Shi,Thomas Gehin,Yann Chevolot,Eliane Souteyrand,Alain Mangé,Jérôme Solassol,Emmanuelle Laurenceau
View all publications

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