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AB78790

Recombinant Human Hsp105/HSP110 protein

4

(1 Review)

|

(2 Publications)

Recombinant Human Hsp105/HSP110 protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

HSP105, HSP110, KIAA0201, HSPH1, Heat shock protein 105 kDa, Antigen NY-CO-25, Heat shock 110 kDa protein, Heat shock protein family H member 1

1 Images
SDS-PAGE - Recombinant Human Hsp105/HSP110 protein (AB78790)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Hsp105/HSP110 protein (AB78790)

12% SDS-PAGE showing ab78790 at approximately 100kDa (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q92598

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.29% Sodium chloride, 0.242% Tris

storage-buffer

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Reactivity data

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

This product was previously labelled as Hsp105
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Sequence info

[{"sequence":"MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLIWNHDSEDTEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEENEMSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQTSQSPPSPELTSEENKIPDADKANEKKVDQPPEAKKPKIKVVNVELPIEANLVWQLGKDLLNMYIETEGKMIMQDKLEKERNDAKNAVEEYVYEFRDKLCGPYEKFICEQDHQNFLRLLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQEAEERPKMFEELGQRLQHYAKIAADFRNKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKKSLDQDPVVRAQEIKTKIKELNNTCEPVVTQPKPKIESPKLERTPNGPNIDKKEEDLEDKNNFGAEPPHQNGECYPNEKNSVNMDLD","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q92598","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

Hsp105 also known as HSP110 is a member of the heat shock protein family. With a molecular mass of approximately 105 kDa this protein functions as a molecular chaperone. It assists in the proper folding of proteins and prevents aggregation especially under stress conditions. Hsp105 is expressed in various tissues including the brain heart and skeletal muscles indicating its widespread roles in maintaining cellular protein homeostasis.
Biological function summary

Hsp105 plays an essential role in protein folding and stress responses. It forms part of a cellular complex that includes other chaperones like Hsp70 and Hsp40. This interaction is critical in refolding denatured proteins and preventing the accumulation of misfolded proteins. In the cell the chaperone activity of Hsp105 helps in managing protein quality control particularly during heat shock and other stress conditions.

Pathways

This protein integrates within signaling cascades associated with stress responses and apoptosis. It is an important player in the HSF1-mediated heat shock response pathway which regulates the expression of various heat shock proteins. Additionally Hsp105 interacts with proteins like Hsp70 within this pathway coordinating cellular mechanisms that protect against protein-damaging conditions. Another pathway in which Hsp105 is involved might be the ubiquitin-proteasome pathway facilitating the degradation of damaged proteins.

Hsp105 has connections to neurodegenerative disorders and cancer. Studies show that its overexpression may link to tumor resistance against chemotherapy by stabilizing proteins involved in cell survival pathways. In neurodegenerative diseases like Alzheimer's Hsp105 binds to tau proteins potentially impacting their normal function and aggregation. It works alongside related proteins such as Hsp70 in these contexts highlighting its role in the pathogenesis and progression of these diseases.
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Specifications

Form

Liquid

Additional notes

ab78790 is purified using conventional chromatography techniques.

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General info

Function

Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (PubMed : 24318877). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity).

Sequence similarities

Belongs to the heat shock protein 70 family.

Post-translational modifications

Phosphorylation on Ser-509 may be important for regulation of the HSPA8/HSC70 chaperone activity.

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (PubMed : 24318877). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity).
See full target information HSPH1
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Publications (2)

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

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 30:564-77 PubMed26443817

2015

Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response.

Applications

Unspecified application

Species

Unspecified reactive species

Adahir Labrador-Garrido,Marta Cejudo-Guillén,Soumya Daturpalli,María M Leal,Rebecca Klippstein,Erwin J De Genst,Javier Villadiego,Juan J Toledo-Aral,Christopher M Dobson,Sophie E Jackson,David Pozo,Cintia Roodveldt
View all publications
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Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions
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Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

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