adha
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Bacillus subtilis | ADHA-1225B | Recombinant Bacillus subtilis ADHA protein, His-tagged | E. coli or Yeast | His |
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Q&As (10)
Ask a questionADHA exhibits a specific cellular localization, with distinct distribution within various subcellular compartments, indicating its functional relevance in those locations.
Besides its known enzymatic activity, ADHA may catalyze additional reactions with physiological consequences, expanding its functional repertoire.
ADHA is implicated in specific physiological processes or signaling pathways, and uncovering the underlying molecular mechanisms advances our understanding of its function.
Investigating the three-dimensional structure of ADHA offers insights into its catalytic mechanism, protein interactions, and potential target sites for modulation.
Pharmacological targeting or modulation of ADHA holds potential for therapeutic applications, making it an attractive target for drug development in relevant disorders or conditions.
Post-translational modifications on ADHA can influence its stability, localization, or enzymatic activity, highlighting their regulatory role in its function.
The expression of ADHA is subject to regulation during development and in response to specific stimuli, shedding light on its dynamic expression patterns.
ADHA possesses enzymatic activity, and understanding its specific substrates and products provides valuable information on its biochemical role.
ADHA has the potential to interact with specific proteins or engage in protein-protein interactions, indicating its involvement in complex cellular processes.
Functional domains or motifs within the ADHA protein contribute to its biological activity, providing insights into its structure-function relationship.
Customer Reviews (2)
Write a reviewShows outstanding specificity in inhibiting the activity of target enzymes in enzymatic inhibition assays.
Highly sensitive in detecting protein phosphorylation events in phosphoproteomics analysis.
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