Rabbit Recombinant Monoclonal Hsp105/HSP110 antibody - conjugated to Alexa Fluor® 555.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
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).
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
Rabbit Recombinant Monoclonal Hsp105/HSP110 antibody - conjugated to Alexa Fluor® 555.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.
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.
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.
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.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
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