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Human Beta-glucuronidase/GUSB Recombinant Protein (His tag)

SKU:
RPES6006
Product Type:
Recombinant Protein
Species:
Human
€499
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Description

Product Name:Human Beta-glucuronidase/GUSB Recombinant Protein (His tag)
Product Code:RPES6006
Size:20µg
Species:Human
Expression Host:HEK293 Cells
Synonyms:Beta-glucuronidase, EC 3.2.1.31, Beta-G1, GUSB
Mol Mass:71.5 kDa
AP Mol Mass:80 kDa
Tag:C-His
Purity:> 95 % as determined by reducing SDS-PAGE.
Endotoxin Level:Please contact us for more information.
Bio Activity:Testing in progress
Sequence:Met1-Thr651
Accession:P08236
Storage:Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Shipping:This product is provided as lyophilized powder which is shipped with ice packs.
Formulation:Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution:Please refer to the printed manual for detailed information.
Background:Human beta -Glucuronidase (EC 3.2.1.31) encoded by the GUSB gene is a lysosomal hydrolase involved in the stepwise degradation of glucuronic acid-containing glycosaminoglycans that include heparan sulfate, chondroitin sulfate and hyaluronan. The enzyme is only active on the glucuronic acid of the non-reducing end. The native protein has been reported as a tetrameric glycoprotein composed of identical subunits. Mutations in the GUSB gene are linked to mucopolysaccharidosis type VII. Accumulation of partially degraded glycosaminoglycans, with glucuronic acid residues at the non-reducing termini, are usually found in the lysosomes of patients with the disease. It has also been reported that this enzyme may contribute to the depletion of chondroitin from cartilage and thereby facilitate the damage of joints in rheumatoid arthritis.

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