Rhodamine 110 CAS 13558-31-1

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Physical properties

Molecular weight	366.8
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	12171501

Overview SDS Protocol

CAS

13558-31-1

Molecular weight

366.8

Extinction coefficient (cm ^-1 M ^-1)

80000

Excitation (nm)

500

Emission (nm)

522

Rhodamine 110 (R110) is the precursor for a variety of R110-based enzyme substrates. It is also used as a calibration standard for R110-based enzyme substrates. Compared to AMC and AFC enzyme substrates, fluorogenic R110 substrates are generally more sensitive, giving longer absorption and fluorescence wavelength than AMC and AFC substrates.

Calculators

Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of Rhodamine 110 *CAS 13558-31-1* 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	272.628 µL	1.363 mL	2.726 mL	13.631 mL	27.263 mL
5 mM	54.526 µL	272.628 µL	545.256 µL	2.726 mL	5.453 mL
10 mM	27.263 µL	136.314 µL	272.628 µL	1.363 mL	2.726 mL

Molarity calculator

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Mass (Calculate)		Molecular weight		Volume (Calculate)		Concentration (Calculate)		Moles
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Spectrum

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Spectral properties

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

Product Family

Name	Excitation (nm)	Emission (nm)	Extinction coefficient (cm ^-1 M ^-1)
Rhodamine 800 CAS 137993-41-0	682	704	-
Rhodamine B CAS 81-88-9	546	567	106000¹
Rhodamine 6G CAS 989-38-8	525	548	116000¹
Rhodamine 123 CAS 62669-70-9	508	528	85200
Rhodamine aldehyde [5-TAMRA aldehyde]	552	578	90000

Images

Figure 1. Chemical structure for Rhodamine 110 *CAS 13558-31-1*

Citations

View all 1 citations: Citation Explorer

Phosphatase-degradable Nanoparticles: A game-changing approach for the delivery of antifungal proteins
Authors: Akku{\c{s}}-Da{\u{g}}deviren, Zeynep Burcu and Saleh, Ahmad and Sch{\"o}pf, Cristina and Truszkowska, Martyna and Bratschun-Khan, Doris and F{\"u}rst, Andrea and Seybold, Anna and Offterdinger, Martin and Marx, Florentine and Bernkop-Schn{\"u}rch, Andreas
Journal: Journal of Colloid and Interface Science (2023)

References

View all 8 references: Citation Explorer

N-DEVD-N'-morpholinecarbonyl-rhodamine 110: novel caspase-3 fluorogenic substrates for cell-based apoptosis assay
Authors: Wang ZQ, Liao J, Diwu Z.
Journal: Bioorg Med Chem Lett (2005): 2335

A transgenic mouse model with a luciferase reporter for studying in vivo transcriptional regulation of the human CYP3A4 gene
Authors: Zhang W, Purchio AF, Chen K, Wu J, Lu L, Coffee R, Contag PR, West DB.
Journal: Drug Metab Dispos (2003): 1054

Fluorogenic substrate [Ala-Pro]2-cresyl violet but not Ala-Pro-rhodamine 110 is cleaved specifically by DPPIV activity: a study in living Jurkat cells and CD26/DPPIV-transfected Jurkat cells
Authors: Boonacker E, Elferink S, Bardai A, Fleischer B, Van Noorden CJ.
Journal: J Histochem Cytochem (2003): 959

Design and synthesis of rhodamine 110 derivative and caspase-3 substrate for enzyme and cell-based fluorescent assay
Authors: Cai SX, Zhang HZ, Guastella J, Drewe J, Yang W, Weber E.
Journal: Bioorg Med Chem Lett (2001): 39

Rhodamine 110-linked amino acids and peptides as substrates to measure caspase activity upon apoptosis induction in intact cells
Authors: Hug H, Los M, Hirt W, Debatin KM.
Journal: Biochemistry (1999): 13906

Intracellular accumulation of rhodamine 110 in single living cells
Authors: Jeannot V, Salmon JM, Deumie M, Viallet P.
Journal: J Histochem Cytochem (1997): 403

Flow cytometric determination of aminopeptidase activities in viable cells using fluorogenic rhodamine 110 substrates
Authors: Ganesh S, Klingel S, Kahle H, Valet G.
Journal: Cytometry (1995): 334

Flow cytometric determination of cysteine and serine proteinase activities in living cells with rhodamine 110 substrates
Authors: Klingel S, Rothe G, Kellermann W, Valet G.
Journal: Methods Cell Biol (1994): 449