Recombinant Human Glucosylceramidase/GBA Protein, CF



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Recombinant Human Glucosylceramidase/GBA Protein, CF Summary

Details of Functionality
Measured by its ability to hydrolyze 4-methylumbelliferyl-beta -D-glucopyranoside. The specific activity is >180 pmol/min/μg, as measured under the described conditions.
Chinese Hamster Ovary cell line, CHO-derived human Glucosylceramidase/GBA protein
Met1-Gln536, with C-terminal 6-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Enzymes
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


Theoretical MW
56 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
58-75 kDa, reducing conditions
Read Publications using
7410-GH in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Supplied as a 0.2 μm filtered solution in Tris, NaCl, Glycerol and DTT.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Assay Procedure
  • Assay Buffer: 50 mM Sodium Citrate, 25 mM Sodium Cholate, 5 mM DTT, pH 6.0
  • Stop Solution: 0.5 M Glycine, 0.3 M NaOH (~pH 10.0)
  • Recombinant Human Glucosylceramidase/GBA (rhGBA) (Catalog # 7410-GH)
  • Substrate: 4-methylumbelliferyl-beta -D-glucopyranoside (Sigma, Catalog # M3633), 10 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhGBA to 0.4 ng/μL in Assay Buffer.
  2. Dilute Substrate to 6 mM in Assay Buffer.
  3. Load in a plate 25 μL of 0.4 ng/μL rhGBA, and start the reaction by adding 25 μL of 6 mM Substrate. Include a Substrate Blank containing 25 μL of Assay Buffer and 25 μL of 6 mM Substrate.
  4. Seal plate and incubate at 37 °C for 20 minutes.
  5. After incubation, stop the reactions by adding 50 μL of Stop Solution to each well.
  6. Read at excitation and emission wavelengths of 365 nm and 445 nm (top read), respectively, in endpoint mode.
  7. Calculate specific activity: 

     Specific Activity (pmol/min/µg) =

Adjusted Fluorescence* (RFU) x Conversion Factor** (pmol/RFU)
Incubation time (min) x amount of enzyme (µg)

     *Adjusted for Substrate Blank
     **Derived using calibration standard 4-methylumbelliferone (Sigma, Catalog # 69580).

  • rhGBA: 0.010 μg
  • Substrate: 1.5 mM


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Glucosylceramidase/GBA Protein, CF

  • Acid beta-glucosidase
  • Alglucerase
  • beta-glucocerebrosidase
  • D-glucosyl-N-acylsphingosine glucohydrolase
  • EC
  • GBA
  • GBA1
  • GC
  • GCB
  • GLUC
  • glucosidase, beta, acid
  • glucosidase, beta; acid (includes glucosylceramidase)
  • Glucosylceramidase
  • Imiglucerase
  • lysosomal glucocerebrosidase


Glucosylceramidase is a lysosomal enzyme that cleaves the beta-glucosidic linkage of glucosylceramide (1, 2), an intermediate in glycolipid metabolism. The mature enzyme has 497 amino acids with a molecular weight of 62 kDa (3). Glycosylation occurs at four of five N-glycosylation sites and is essential for the trafficking and activity of the enzyme (4). The enzyme is activated in lysosomes by saposin C, although the mechanism of activation is not well understood (5). Defects in Glucosylceramidase are the cause of Gaucher disease, also known as glucocerebrosidase deficiency (6). Gaucher disease is the most prevalent lysosomal storage disease, characterized by accumulation of glucosylceramide in the reticulo-endothelial system. Symptoms of Gaucher disease may include enlarged spleen and liver, liver malfunction, skeletal disorders and bone lesions, severe neurologic complications, swelling of lymph nodes, anemia, low blood platelets and yellow fatty deposits on the white of the eye (7). Currently, enzyme replacement therapy is used to treat patients with the disease (8, 9).
  1. Sorge, J. et al. (1985) Proc. Natl. Acad. Sci. USA 82:7289.
  2. Ginns, E. I. et al. (1984) Biochem. Biophyl. Res. Commun. 123:574.
  3. Horowitz, M. et al. (1989) Genomics 4:87.
  4. Grace, M.E. et al. (1994) J. Biol. Chem. 269:2283.
  5. Bruhn, h. (2005) Biochem. J. 389:249.
  6. Liou, B. et al. (2006) J. Biol. Chem. 281:4242.
  7. Grabowski, G.A. (2008). Lancet 372: 1263–1271.
  8. Zheng, W. et al. (2007) Proc. Natl. Acad. Sci. USA 104:13192.
  9. Beutler, E. and Gelbart, T. (1996) Hum. Mutat. 8:207.

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Gene Symbol GBA