Recombinant Human Galactosylceramidase/GALC Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7310-GH

R&D Systems, part of Bio-Techne
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7310-GH-005
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Key Product Details

Source

CHO

Accession #

NP_000144

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Galactosylceramidase/GALC Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Galactosylceramidase/GALC protein
Met1-Arg685, with a C-terminal 6-His tag

Purity

>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Tyr43

Predicted Molecular Mass

74 kDa

SDS-PAGE

70-85 kDa, reducing conditions

Activity

Measured by its ability to cleave a fluorogenic substrate, 4-Methylumbelliferyl-beta -D-galactopyranoside.
The specific activity is >550 pmol/min/ug, as measured under the described conditions.

Reviewed Applications

Read 1 review rated 5 using 7310-GH in the following applications:

Scientific Data Images for Recombinant Human Galactosylceramidase/GALC Protein, CF

Recombinant Human Galactosylceramidase/GALC Protein Enzyme Activity Diagram.

Recombinant Human Galactosylceramidase/GALC Protein Enzyme Activity Diagram. Recombinant Human Galactosylceramidase/GALC Protein, CF (Catalog # 7310-GH) catalyzes the hydrolysis of beta-d-galactocerebroside to beta-d-galactose and ceramide.

Recombinant Human Galactosylceramidase/GALC Protein Enzyme Activity.

Recombinant Human Galactosylceramidase/GALC Protein, CF (Catalog # 7310-GH) is measured by its ability to cleave a fluorogenic substrate, 4-Methylumbelliferyl-beta -D-galactopyranoside.

Recombinant Human Galactosylceramidase/GALC Protein SDS-PAGE.

2 μg/lane of Recombinant Human Galactosylceramidase/GALC Protein (Catalog # 7310-GH) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 70-85 kDa.

Formulation, Preparation and Storage

7310-GH
Formulation Supplied as a 0.2 μm filtered solution in MES, NaCl and Glycerol.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Galactosylceramidase/GALC

Galactosylceramidase (GALC or galactocerebrosidase) is a lysosomal enzyme that hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride, molecules that are important in the production of normal myelin (1). Mutations in the GALC gene have been associated with Krabbe’s Disease, also known as globoid cell leukodystrophy (2, 3, 4), a fatal autosomal recessive disorder resulting from the insufficient catabolism of these galactolipids. Krabbe’s Disease is morphologically characterized by almost total absence of myelin, severe gliosis, and the presence of characteristic multinucleated globoid cells in the white matter (4). In a recent study, cord blood transplants have been successful in stopping the disease (5).

References

  1. Chen, Y.Q. et al. (1993) Hum. Mol. Genet. 2:1841.
  2. Tappino, B. et al. (2010) Hum. Mutat. 31:E1894.
  3. Kodama, S. et al. (1982) J Neurochem. 39:1314.
  4. Suzuki, K. and Suzuki, Y. (1970) Proc. Natl. Acad. Sci. U.S.A. 66:302.
  5. Escolar, M.L. et al. (2005) N. Engl. J. Med. 352:2069.

Alternate Names

Galactocerebrosidase, Galactocerebroside beta-galactosidase, Galactosylceraminidase, GALC

Entrez Gene IDs

2581 (Human); 14420 (Mouse); 314360 (Rat)

Gene Symbol

GALC

UniProt

NP_000144

Additional Galactosylceramidase/GALC Products

Product Documents for Recombinant Human Galactosylceramidase/GALC Protein, CF

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Certificate of Analysis

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Product Specific Notices for Recombinant Human Galactosylceramidase/GALC Protein, CF

For research use only

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