Abcam, ab307717, Anti-AHA1 antibody [EPR26852-47] - BSA and Azide free

Size: 100µg / 1mg
Rabbit Recombinant Monoclonal AHA1 antibody. Carrier free. Suitable for WB, IP and reacts with Human, Mouse, Rat samples.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR26852-47,
Isotype:IgG,
Carrier free:Yes,
Reacts with:Human, Mouse, Rat,
Applications: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
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
AHA1 also known as activator of heat shock 90kDa protein ATPase homolog 1 is a co-chaperone protein that plays a role in the regulation of HSP90 ATPase activity. This protein has a molecular weight of approximately 38 kDa. AHA1 expression occurs in various tissues with higher amounts seen in metabolically active tissues. It interacts directly with HSP90 enhancing the chaperone's ability to fold client proteins correctly by stimulating its ATPase activity.
Biological function summary
AHA1 modulates the function of the HSP90 chaperone complex. This complex is important for the stabilization and activation of many client proteins such as steroid hormone receptors and kinases. AHA1 binds to the middle domain of HSP90 contributing to conformational changes necessary for efficient ATP hydrolysis. By influencing these molecular processes AHA1 plays a role in maintaining cellular protein homeostasis under stress conditions.
Pathways
The HSP90-AHA1 interaction is significant in the signaling pathway of cellular stress responses and protein folding. AHA1's upregulating effect on HSP90 ATPase activity facilitates the correct folding and function of client proteins involved in the MAPK/ERK and PI3K/AKT pathways. These pathways commonly involve interactions with proteins such as RAF and PI3K which are important in cell proliferation and survival processes.
AHA1 influences the progression of cancer and neurodegenerative diseases. Altered expression or function of AHA1 is linked to the development and progression of cancer as it affects the stability of oncoproteins through its interaction with HSP90. The protein is also connected to neurodegenerative diseases with disruptions in its function or expression impacting the folding and maintenance of neuronal proteins. In these diseases the AHA1-HSP90 interaction remains a critical component of pathogenic pathways affecting disease manifestation and progression.