AHA1, His-tag Recombinant

What it means: E. coli — this protein was produced in E. coli, determining its post-translational modification profile and application suitability.

Why it matters:

• Insect cell (Sf9) systems support post-translational processing required for kinase activity and complex formation; HEK293 supports human-like glycosylation; E. coli yields high-quantity non-glycosylated protein.
• For assays measuring native enzymatic activity (kinase, phosphodiesterase, deacetylase), the expression system directly affects the quality and accuracy of results.

How to interpret here: Verify E. coli is compatible with your assay requirements, particularly for enzyme kinetics and cell-based applications.

What it means: C-terminal His-tag — this affinity tag enables one-step chromatographic purification and can serve as a detection epitope.

Why it matters:

• GST-tag enables glutathione-affinity pull-down assays; His-tag enables IMAC and is compatible with anti-His detection; Avi-tag enables site-specific biotinylation for SPR/BLI capture or streptavidin-based assays; Fc-tag enables protein A/G purification and can extend half-life.
• Tag position (N- vs C-terminal) may affect domain accessibility — verify it does not occlude the active site or binding interface.

How to interpret here: Use anti-C antibodies for tag-based detection or capture in pull-down and ELISA assays.

What it means: Not applicable (BSL-1) — this protein has been classified under BSL-1 safety requirements, the lowest biosafety classification.

Why it matters:

• BSL-1 proteins pose no known risk to healthy adult laboratory workers and do not require specialised containment or personal protective equipment beyond standard laboratory practice.
• Confirms suitability for use in standard biochemistry or molecular biology laboratories without institutional BSL-2 or higher facility requirements.

How to interpret here: Standard laboratory safety practices apply. Review the product SDS/Datasheet for handling precautions specific to this compound.

What it means: This protein spans amino acids full length of the target protein, covering the region used for expression and purification.

Why it matters:

• The expressed amino acid region determines which functional domains are present — catalytic domains, binding interfaces, or regulatory regions — affecting activity and assay design.
• For fragment proteins, confirm the region includes your domain of interest (active site, binding pocket, substrate site) before ordering.

How to interpret here: Amino acids full length are included in this construct. Cross-reference with the UniProt domain annotation to confirm coverage of your target region.

What it means: The addition of AHA1 increased ATPase activity of HSP90alpha from 0.18 to 0.94 pmol/min/µg. — specific activity quantifies the catalytic potency of the protein per unit mass.

Why it matters:

• High specific activity indicates correctly folded, fully active protein, reducing the amount required per assay and improving signal-to-noise in screening campaigns.
• Lot-to-lot specific activity consistency ensures reproducible IC50 values across screening runs and between project teams.

How to interpret here: The stated specific activity was determined under defined assay conditions (see datasheet). Optimise substrate concentrations and incubation times to achieve the dynamic range needed for your inhibitor screening application.

What it means: UniProt accession O95433 is the canonical identifier for this protein in the Universal Protein Resource database.

Why it matters:

• UniProt provides the canonical sequence, domain architecture, known mutations, disease associations, and curated literature — essential for designing inhibitor assays.
• Use the accession for database cross-referencing in publications and to identify known binding partners and substrate sequences.

How to interpret here: Visit uniprot.org/O95433 to retrieve the full protein sequence, verify the expressed amino acid region, and review annotated active site residues and known inhibitors.