AHSA1L
| Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| Zebrafish | AHSA1L-11881Z | Recombinant Zebrafish AHSA1L | Mammalian Cell | His |
|
- Involved Pathway
- Protein Function
- Interacting Protein
AHSA1L involved in several pathways and played different roles in them. We selected most pathways AHSA1L participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with AHSA1L were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
AHSA1L has several biochemical functions, for example, ATPase activator activity, chaperone binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AHSA1L itself. We selected most functions AHSA1L had, and list some proteins which have the same functions with AHSA1L. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| ATPase activator activity | DNAJC19;DNAJC24;AHSA1;DNAJC15;DNAJC10;ATP1B2;RAB4A;AHSA1L;MYBPC3 |
| chaperone binding | HSP104;DNAJC10;BIRC5;TIMM44;DNAJC3;BAG5;VWF;GRPEL2;HSPE1 |
AHSA1L has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AHSA1L here. Most of them are supplied by our site. Hope this information will be useful for your research of AHSA1L.
- Q&As
- Reviews
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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