Recombinant Zebrafish AHSA1

• Cat.No.: AHSA1-4140Z
• Product Overview: Recombinant Zebrafish AHSA1 full length or partial length protein was expressed.

Specification

• Source: Mammalian Cells
• Species: Zebrafish
• Tag: His
• Form: Liquid or lyophilized powder
• Endotoxin: < 1.0 eu per μg of the protein as determined by the LAL method.
• Purity: >80%
• Notes: This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.
• Storage: Store it at +4 oC for short term. For long term storage, store it at -20 oC～-80 oC.
• Storage Buffer: PBS buffer

Gene Information

• Gene Name: ahsa1 AHA1, activator of heat shock protein ATPase homolog 1 (yeast) [ Danio rerio (zebrafish) ]
• Official Symbol: AHSA1
• Gene ID: 565968
• mRNA Refseq: NM_001045091
• Protein Refseq: NP_001038556
• UniProt ID: Q5RIK5

Reviews

01/17/2022

Top-quality item well worth the price. Supportive customer service.

12/23/2021

Affordable yet exceptional quality. Customer service made the process easy.

04/05/2020

Quality met the price point, and the customer service was exceptional.

06/09/2019

Received superb customer service and a premium product at a fair price.

09/28/2018

Product quality justified the cost, and the customer service was excellent.

Q&As

How does AHSA1 regulate the chaperone activity of HSP90?

AHSA1 stimulates the ATPase activity of HSP90, enhancing its chaperone function and facilitating the folding, stabilization, and maturation of client proteins.

How does AHSA1's activity contribute to the conformational changes of HSP90 during the chaperone cycle?

AHSA1 promotes conformational changes in HSP90 that enhance its ATPase activity, facilitating the release of client proteins at different stages of folding.

What is the role of AHSA1 in protein trafficking and localization within cells?

AHSA1 assists in proper folding of proteins destined for specific cellular compartments, contributing to their accurate localization.

How can structural biology techniques, such as cryo-electron microscopy, contribute to understanding AHSA1's mechanism of action?

These techniques can reveal the complex architecture of the AHSA1-HSP90 complex and provide insights into the conformational changes it undergoes during its chaperone cycle.

In the lab, what methods are used to study the dynamic changes in AHSA1 expression and its interaction with HSP90 under stress?

Western blotting, immunofluorescence microscopy, and proximity ligation assays can be employed to study AHSA1 expression and its colocalization with HSP90 in stressed cells.

How is the interaction between AHSA1 and HSP90 characterized at the molecular level?

Techniques like co-immunoprecipitation, surface plasmon resonance, and X-ray crystallography provide insights into the AHSA1-HSP90 interaction.

What biochemical assays are used to measure the ATPase-stimulating activity of AHSA1 on HSP90?

Assays like malachite green or colorimetric methods can be used to quantify the release of inorganic phosphate, indicative of ATP hydrolysis, in the presence of AHSA1 and HSP90.

How can the AHSA1-HSP90 complex be targeted for therapeutic interventions?

Small molecules that disrupt the AHSA1-HSP90 interaction could be designed to interfere with client protein folding and impact disease-associated pathways.

What are some examples of client proteins that depend on the AHSA1-HSP90 complex for proper folding and function?

Client proteins include various kinases, steroid hormone receptors, and transcription factors involved in cell signaling and gene regulation.

How does AHSA1 influence the assembly of multi-protein complexes involved in cellular signaling pathways?

AHSA1 can stabilize and facilitate the correct assembly of multi-protein complexes, thereby modulating cellular signaling cascades.