| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Lysosomal acid Glucosylceramidase (Gba1); (Lysosomal acid GCase)(Acid beta-glucosidase)(Beta-glucocerebrosidase)(Cholesterol glucosyltransferase)(SGTase)(Cholesteryl-beta-glucosidase)(D-glucosyl-N-acylsphingosine glucohydrolase)(Lysosomal cholesterol glycosyltransferase)(Lysosomal galactosylceramidase)(Lysosomal glycosylceramidase) |
| Conjugate | |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Reconstitution | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Overview
Recombinant Mouse Lysosomal acid Glucosylceramidase (Gba1) is a recombinant protein reagent derived from Mus musculus (Mouse) and produced in E.coli. It is commonly used to support Metabolism research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.
Key elements and design rationale
- Expressed region: 20-515aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
- Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
- Tag / fusion: Tag-Free. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
- Molecular weight (reported): 55.6 kDa. Apparent size may vary with tags, processing, and gel conditions.
When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.
Biological background
The gene commonly associated with this target is Gba1. Gba1 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Mus musculus (Mouse) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.
Research relevance and current trends
- Quantifying enzyme activity, substrate specificity, and cofactor dependence in metabolic pathways.
- Connecting metabolic state to cellular phenotypes using targeted protein reagents and quantitative assays.
- Integrating multi-omics measurements with protein-level readouts to refine pathway models and regulatory mechanisms.
Relevance: Acid beta-glucosidase Beta-glucocerebrosidase D-glucosyl-N-acylsphingosine glucohydrolase
Common research applications
- Assay and standard development for immunoassays or binding-based detection methods.
- Protein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.
- Structure–function analysis, including domain mapping or evaluation of sequence variants.
In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.
Notes for experimental interpretation
- Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
- Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
- Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
- E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.
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