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Bis-L-Aspartic acid Beta-rhodamine 110
Bis-L-Aspartic acid β-rhodamine 110 is a sensitive fluorogenic substrate for studying lysosomal glycoasparaginases (aspartylglucosaminidases) and L-asparaginases. It is used for the assays for lysosomal glycoasparaginase (aspartylglucosaminidase) activity and the diagnosis of aspartylglucosaminuria. Aspartylglucosaminidase is an amidohydrolase enzyme involved in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves asparagine from N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins. The lysosomal storage disease aspartylglycosaminuria is caused by a deficiency in the AGA enzyme.
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Common stock solution preparation
Table 1. Volume of DMSO needed to reconstitute specific mass of Bis-L-Aspartic acid Beta-rhodamine 110 to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.
| 0.1 mg | 0.5 mg | 1 mg | 5 mg | 10 mg | |
| 1 mM | 126.812 µL | 634.059 µL | 1.268 mL | 6.341 mL | 12.681 mL |
| 5 mM | 25.362 µL | 126.812 µL | 253.624 µL | 1.268 mL | 2.536 mL |
| 10 mM | 12.681 µL | 63.406 µL | 126.812 µL | 634.059 µL | 1.268 mL |
Molarity calculator
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Citations
View all 6 citations: Citation Explorer
Chromosomal localization of the human glycoasparaginase gene to 4q32-q33
Authors: Morris, C., Heisterkamp, N., Groffen, J., Williams, J. C., Mononen, I.
Journal: Hum Genet (1992): 295-7
Authors: Morris, C., Heisterkamp, N., Groffen, J., Williams, J. C., Mononen, I.
Journal: Hum Genet (1992): 295-7
Substrate specificity and reaction mechanism of human glycoasparaginase. The N-glycosidic linkage of various glycoasparagines is cleaved through a reaction mechanism similar to L-asparaginase
Authors: Kaartinen, V., Mononen, T., Laatikainen, R., Mononen, I.
Journal: J Biol Chem (1992): 6855-8
Authors: Kaartinen, V., Mononen, T., Laatikainen, R., Mononen, I.
Journal: J Biol Chem (1992): 6855-8
Splicing defect of the glycoasparaginase gene in two Japanese siblings with apartylglucosaminuria
Authors: Yoshida, K., Yanagisawa, N., Oshima, A., Sakuraba, H., Iida, Y., Suzuki, Y.
Journal: Hum Genet (1992): 179-80
Authors: Yoshida, K., Yanagisawa, N., Oshima, A., Sakuraba, H., Iida, Y., Suzuki, Y.
Journal: Hum Genet (1992): 179-80
Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene
Authors: Mononen, I., Heisterkamp, N., Kaartinen, V., Mononen, T., Williams, J. C., Groffen, J.
Journal: J Biol Chem (1992): 3196-9
Authors: Mononen, I., Heisterkamp, N., Kaartinen, V., Mononen, T., Williams, J. C., Groffen, J.
Journal: J Biol Chem (1992): 3196-9
Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase
Authors: Mononen, I., Heisterkamp, N., Kaartinen, V., Williams, J. C., Yates, J. R., 3rd, Griffin, P. R., Hood, L. E., Groffen, J.
Journal: Proc Natl Acad Sci U S A (1991): 2941-5
Authors: Mononen, I., Heisterkamp, N., Kaartinen, V., Williams, J. C., Yates, J. R., 3rd, Griffin, P. R., Hood, L. E., Groffen, J.
Journal: Proc Natl Acad Sci U S A (1991): 2941-5
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