Abcam, ab109624, Anti-Hsp105/HSP110 antibody [EPR4576]

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal Hsp105/HSP110 antibody. Suitable for IHC-P, IP, WB, ICC/IF and reacts with Human, Mouse, Rat samples. Cited in 19 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR4576,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Rat, Human,
Applications:IHC-P, ICC/IF, WB, IPSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Stable for 12 months at -20°C

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.