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Bis-L-Aspartic acid Beta-rhodamine 110

Chemical structure for Bis-L-Aspartic acid Beta-rhodamine 110.
Chemical structure for Bis-L-Aspartic acid Beta-rhodamine 110.
Ordering information
Price ()
Catalog Number13480
Unit Size
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Additional ordering information
Telephone1-408-733-1055
Fax1-408-733-1304
Emailsales@aatbio.com
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ShippingStandard overnight for United States, inquire for international
Physical properties
Molecular weight788.57
SolventDMSO
Spectral properties
Extinction coefficient (cm -1 M -1)80000
Excitation (nm)500
Emission (nm)522
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12352200
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Show More (57)

OverviewpdfSDSpdfProtocol


See also: Enzymes, 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 mg0.5 mg1 mg5 mg10 mg
1 mM126.812 µL634.059 µL1.268 mL6.341 mL12.681 mL
5 mM25.362 µL126.812 µL253.624 µL1.268 mL2.536 mL
10 mM12.681 µL63.406 µL126.812 µL634.059 µL1.268 mL

Molarity calculator

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Spectrum


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spectrum

Spectral properties

Extinction coefficient (cm -1 M -1)80000
Excitation (nm)500
Emission (nm)522

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
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
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
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
Glycoasparaginase in human urine
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