Bis-L-Aspartic acid Beta-rhodamine 110
Ordering information
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Additional ordering information
| Telephone | 1-800-990-8053 |
| Fax | 1-800-609-2943 |
| sales@aatbio.com | |
| International | See distributors |
| Bulk request | Inquire |
| Custom size | Inquire |
| Shipping | Standard overnight for United States, inquire for international |
Physical properties
| Molecular weight | 788.57 |
| Solvent | DMSO |
Spectral properties
| Extinction coefficient (cm -1 M -1) | 80000 |
| Excitation (nm) | 500 |
| Emission (nm) | 522 |
Storage, safety and handling
| H-phrase | H303, H313, H333 |
| Hazard symbol | XN |
| Intended use | Research Use Only (RUO) |
| R-phrase | R20, R21, R22 |
| Storage | Freeze (< -15 °C); Minimize light exposure |
| UNSPSC | 12352200 |
Related products
| Overview |  SDSProtocol |
See also: Proteases
Molecular weight 788.57 | Extinction coefficient (cm -1 M -1) 80000 | Excitation (nm) 500 | Emission (nm) 522 |
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.
Calculators
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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Spectrum
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Spectral properties
| Extinction coefficient (cm -1 M -1) | 80000 |
| Excitation (nm) | 500 |
| Emission (nm) | 522 |
Images
Figure 1. Chemical structure for Bis-L-Aspartic acid Beta-rhodamine 110.
Citations
View all 6 citations: Citation Explorer
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
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
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
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
Glycoasparaginase in human urine
Authors: Kaartinen, V.
Journal: Biochim Biophys Acta (1991): 28-30
Authors: Kaartinen, V.
Journal: Biochim Biophys Acta (1991): 28-30
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
Application notes
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