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AB78790

Recombinant Human Hsp105/HSP110 protein (His tag N-Terminus)

Recombinant Human Hsp105/HSP110 protein (His tag N-Terminus)

4

(1 Review)

|

(2 Publications)

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

別名を表示する

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 (His tag N-Terminus) (AB78790)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Hsp105/HSP110 protein (His tag N-Terminus) (AB78790)

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

Key facts

精製度

>90% SDS-PAGE

発現系

Escherichia coli

タグ

His tag N-Terminus

アプリケーション

SDS-PAGE

applications

生物活性

No

アクセッション番号

Q92598

アニマルフリー

No

キャリアフリー

No

Human

バッファー組成

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

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>" } } }

製品の詳細

This product was previously labelled as Hsp105

配列情報

[{"sequence":"MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLIWNHDSEDTEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEENEMSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQTSQSPPSPELTSEENKIPDADKANEKKVDQPPEAKKPKIKVVNVELPIEANLVWQLGKDLLNMYIETEGKMIMQDKLEKERNDAKNAVEEYVYEFRDKLCGPYEKFICEQDHQNFLRLLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQEAEERPKMFEELGQRLQHYAKIAADFRNKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKKSLDQDPVVRAQEIKTKIKELNNTCEPVVTQPKPKIESPKLERTPNGPNIDKKEEDLEDKNNFGAEPPHQNGECYPNEKNSVNMDLD","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q92598","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

出荷温度及び保存条件

出荷温度
Blue Ice
短期保存温度
-20°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False

補足情報

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.

製品の性状

製品の状態

Liquid

補足情報

ab78790 is purified using conventional chromatography techniques.

一般的な情報

機能

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).

配列の類似性

Belongs to the heat shock protein 70 family.

翻訳後修飾

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

製品プロトコール

ターゲットの情報

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

文献 (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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