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AB95268

Recombinant Human HspBP1 protein

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Recombinant Human HspBP1 protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

HSPBP, PP1845, HSPBP1, Hsp70-binding protein 1, HspBP1, Heat shock protein-binding protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 1, Hsp70-interacting protein 2, HspBP2

1 Images
SDS-PAGE - Recombinant Human HspBP1 protein (AB95268)
  • SDS-PAGE

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SDS-PAGE - Recombinant Human HspBP1 protein (AB95268)

15% SDS-PAGE analysis of 3μg ab95268.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9NZL4

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 30% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0584% EDTA, 0.0308% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

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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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSDEGSRGSRLPLALPPASQGCSSGGGGGGGGGSSAGGSGNSRPPRNLQGLLQMAITAGSEEPDPPPEPMSEERRQWLQEAMSAAFRGQREEVEQMKSCLRVLSQPMPPTAGEAEQAADQQEREGALELLADLCENMDNAADFCQLSGMHLLVGRYLEAGAAGLRWRAAQLIGTCSQNVAAIQEQVLGLGALRKLLRLLDRDACDTVRVKALFAISCLVREQEAGLLQFLRLDGFSVLMRAMQQQVQKLKVKSAFLLQNLLVGHPEHKGTLCSMGMVQQLVALVRTEHSPFHEHVLGALCSLVTDFPQGVRECREPELGLEELLRHRCQLLQQHEEYQEELEFCEKLLQTCFSSPADDSMDR","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9NZL4","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.

HspBP1 also known as Heat Shock Protein Binding Protein 1 acts mechanically as a co-chaperone that regulates the activity of Hsp70. It has a molecular mass of approximately 28 kDa. HspBP1 expression occurs in various tissues with significant levels found in tissues undergoing high cellular stress such as the brain and heart. It plays a role in modulating the chaperone activity of Hsp70 by promoting the release of ADP from the nucleotide-binding domain.
Biological function summary

HspBP1 influences protein folding and repair mechanisms in cells. It functions as part of a complex with Hsp70 facilitating the reduction of misfolded and damaged proteins within the cell. Through this interaction HspBP1 assists in maintaining cellular protein homeostasis especially under stressful conditions that might otherwise lead to protein misfolding and aggregation.

Pathways

HspBP1 joins the protein quality control and cellular stress response pathways. Its involvement with Hsp70 is important in these processes ensuring proper protein folding and preventing aggregation. This relationship becomes evident in pathways like the unfolded protein response and heat shock response with HspBP1 modulating activities alongside other chaperones and co-chaperones within these networks.

High or dysfunctional HspBP1 levels associate with neurodegenerative diseases and cancer. In neurodegenerative diseases altered HspBP1 can contribute to the accumulation of misfolded proteins exacerbating conditions such as Alzheimer's disease. Its interaction with Hsp70 is particularly critical in tumorigenesis where enhanced expression can affect tumor progression and therapy resistance.
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Specifications

Form

Liquid

Additional notes

ab95268 is purified using conventional chromatography techniques.

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General info

Function

Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.

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Product protocols

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Target data

Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.
See full target information HSPBP1
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