Name: Bis-L-Aspartic acid Beta-rhodamine 110
Brand: AAT Bioquest
SKU: 13480
Price: 237 USD
Availability: InStock

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.

Datasheet

SDS

COA

Catalog	Size	Price	Quantity
13480	1 mg	Price

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

Enter any two values (mass, volume, concentration) to calculate the third.

Mass (Calculate)		Molecular weight		Volume (Calculate)		Concentration (Calculate)		Moles
mg	÷	788.57 g/mol	=	mL	x	mM	=	mmol

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

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

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

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

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

Physical properties

Molecular weight	788.57
Solvent	DMSO

Spectral properties

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

Usage and storage

Intended use	Research Use Only (RUO)
Storage	Freeze (< -15 °C); Minimize light exposure

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