Purified anti-HSPH1 Antibody, HSPH1, W20247H,BioLegend,678452

For use of this antibody in immunohistochemistry on formalin-fixed paraffin-embedded tissue (IHC-P), it is recommended to perform antigen retrieval using either Citrate Buffer, 10X (Cat. No. 420902) or Tris-EDTA pH 9.0 Antigen Retrieval Buffer (10X) (Cat. No. 422704).It is not recommended to use this product in immunocytochemistry (ICC).

Host

Rat

Reactivity

Human

Application

WB - Quality testedIHC-P - Verified

Platform ID

BAB210488326

BioLegend

Headquarters

8999 BioLegend Way San Diego, CA 92121 United States

Contact

Tel: 1-858-455-9588
Fax: +49 (4131) 7023913

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Product Specifications
Scientific Background

Specifications

NamePurified anti-HSPH1 Antibody, HSPH1, W20247H
Cat. No.678452
HostRat
RRIDAB_3675194 (BioLegend Cat. No. 678451)AB_3675194 (BioLegend Cat. No. 678452)
IsotypeRat IgG2b, κ
ReactivityHuman
ApplicationWB - Quality testedIHC-P - Verified
ClonalityMonoclonal
Clone NumberW20247H
Concentration0.5 mg/mL
TargetHSPH1
ImmunogenRecombinant fragment of human HSPH1
PurityThe antibody was purified by affinity chromatography.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
StorageThe antibody solution should be stored undiluted between 2°C and 8°C.
Regulatory StatusResearch Use Only

Scientific Background

The HSPH1 protein, also known as heat shock protein 105 (HSP105), is a member of the heat shock protein (HSP) family, which plays a crucial role in the maintenance of cellular homeostasis, especially under stress conditions. HSPH1 is a prominent member of the HSP110 family, which is closely related to the HSP70 family but has unique properties and functions. HSPH1 helps to mitigate these harmful effects by functioning as a molecular chaperone, ensuring that denatured proteins refold correctly or are directed towards degradation pathways. This protective mechanism is vital for preventing the accumulation of protein aggregates, which can be toxic and lead to cell death. Studies have shown that HSPH1 can interact with other heat shock proteins, such as HSP70 and HSP40, to form a functional complex that enhances its chaperone activity. Through these interactions, HSPH1 not only prevents protein misfolding but also facilitates the disaggregation of protein aggregates, promoting cellular recovery from stress.HSPH1 is also implicated in various diseases, particularly those associated with protein misfolding and aggregation. For example, neurodegenerative disorders like Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease are characterized by the accumulation of misfolded protein aggregates in neurons. The upregulation of HSPH1 has been suggested as a protective mechanism in these conditions, as it may help reduce the burden of toxic aggregates. HSPH1 has been found to be overexpressed in various cancers, including breast, lung, and colon cancers, where it contributes to the stabilization of oncogenic proteins and supports the survival of cancer cells.

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