| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Non-lysosomal glucosylceramidase (Gba2); partial; (NLGase)(Beta-glucocerebrosidase 2)(Beta-glucosidase 2)(Bile acid beta-glucosidase GBA2)(Bile acid glucosyl transferase GBA2)(Cholesterol glucosyltransferase GBA2)(Cholesteryl-beta-glucosidase GBA2)(Glucosylceramidase 2)(Non-lysosomal cholesterol glycosyltransferase)(Non-lysosomal galactosylceramidase)(Non-lysosomal glycosylceramidase) |
| Conjugate | |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Molecular Weight | |
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| Reconstitution | |
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| UniProt # |
Overview
Recombinant Rat Non-lysosomal glucosylceramidase (Gba2), partial is a recombinant protein reagent derived from Rattus norvegicus (Rat) and produced in E.coli. It is commonly used to support Others research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.
Key elements and design rationale
- Expressed region: 512-877aa. 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: C-terminal 6xHis-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
- Molecular weight (reported): 42.6 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 Gba2. Gba2 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 Rattus norvegicus (Rat) 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
- Using recombinant proteins to enable quantitative binding measurements and reagent benchmarking.
- Studying domain- and isoform-specific effects in pathway models and interaction networks.
- Developing robust, reproducible assays that connect molecular readouts to cellular phenotypes.
Relevance: Non-lysosomal glucosylceramidase that catalyzes the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) to free glucose and ceramides (such as N-acylsphing-4-enine). GlcCers are membrane glycosphingolipids that have a wide intracellular distribution. They are the main precursors of more complex glycosphingolipids that play a role in cellular growth, differentiation, adhesion, signaling, cytoskeletal dynamics and membrane properties. Involved in the transglucosylation of cholesterol, transfers glucose from GlcCer to cholesterol, thereby modifying its water solubility and biological properties. Under specific conditions, may catalyze the reverse reaction, transferring glucose from cholesteryl-3-beta-D-glucoside to ceramide (such as N-acylsphing-4-enine). May play a role in the metabolism of bile acids. Able to hydrolyze bile acid 3-O-glucosides as well as to produce bile acid-glucose conjugates thanks to a bile acid glucosyl transferase activity. Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the galactosyl transfer between GalCers and cholesterol in vitro with lower activity compared with their activity against GlcCers.
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.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
