Recombinant Zebrafish AHSA1L
Cat.No. : | AHSA1L-11881Z |
Product Overview : | Recombinant Zebrafish AHSA1L full length or partial length protein was expressed. |
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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 Name : | ahsa1l AHA1, activator of heat shock protein ATPase homolog 1, like [ Danio rerio (zebrafish) ] |
Official Symbol : | AHSA1L |
Gene ID : | 321945 |
mRNA Refseq : | NM_212602 |
Protein Refseq : | NP_997767 |
UniProt ID : | Q7SXN3 |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (10)
Ask a questionSteps include cell lysis, immunoprecipitation of AHSA1L or Hsp90, protein separation, and subsequent analysis using immunoblotting or mass spectrometry.
Understanding AHSA1L's role in protein folding could lead to tailored therapeutic interventions based on individual protein folding profiles, benefiting personalized medicine approaches.
Fluorescence resonance energy transfer (FRET) and fluorescence anisotropy assays can reveal dynamic interactions between AHSA1L and Hsp90.
AHSA1L contains a TPR (tetratricopeptide repeat) domain that interacts with the C-terminal domain of Hsp90, allowing for co-chaperone complex formation.
AHSA1L contributes to maintaining proper protein folding, preventing misfolding and aggregation, which is crucial for cellular function and health.
AHSA1L's involvement in stabilizing oncogenic client proteins could contribute to the development of drug resistance in cancer cells.
AHSA1L interactions with co-chaperones such as p23 and Hop contribute to the assembly of multi-protein complexes that aid in protein folding.
AHSA1L enhances Hsp90-mediated folding and stabilization of steroid hormone receptors and other client proteins critical for various cellular processes.
AHSA1L binding induces structural changes in Hsp90, enhancing its ATPase activity, which is crucial for the chaperone's conformational cycle.
CRISPR/Cas9-mediated genome editing can be employed to generate AHSA1L knockout cell lines, allowing researchers to study its effects on protein folding pathways.
Customer Reviews (5)
Write a reviewProduct quality exceeded the cost. Customer service was attentive.
Competitive pricing, premium quality, and friendly customer assistance.
Value for money with outstanding customer support.
Affordable pricing, exceptional product quality, and attentive service.
A perfect balance of quality and price. Customer service was fantastic.
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