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5-Carboxytetramethylrhodamine Sale

(Synonyms: 5-羧基四甲基罗丹明) 目录号 : GC64189

A fluorescent dye

5-Carboxytetramethylrhodamine Chemical Structure

Cas No.:150322-05-7

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25 mg
¥450.00
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50 mg
¥720.00
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100 mg
¥1,260.00
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产品描述

5-Carboxytetramethylrhodamine is a fluorescent dye that has commonly been used for the covalent labeling of oligonucleotides for DNA analysis.1 It displays excitation and emission maxima of 546 and 580 nm, respectively.2 5-Carboxytetramethylrhodamine has also been used in various fluorescence polarization assays and protein FRET experiments.2,3

1.Kvach, M.V., Stepanova, I.A., Prokhorenko, I.A., et al.Practical synthesis of isomerically pure 5- and 6-carboxytetramethylrhodamines, useful dyes for DNA probesBioconjug. Chem.20(8)1673-1682(2009) 2.Qi, J., Oppenheimer, M., and Sobrado, P.Fluorescence polarization binding assay for Aspergillus fumigatus virulence factor UDP-galactopyranose mutaseEnzyme Res.513905(2011) 3.Casiraghi, A., Longhena, F., Straniero, V., et al.Design and synthesis of fluorescent-methylphenidate analogues for FRET-based assay of synapsin III bindingChemMedChem15(14)1330-1337(2020)

Chemical Properties

Cas No. 150322-05-7 SDF Download SDF
别名 5-羧基四甲基罗丹明
分子式 C25H22N2O5 分子量 430.45
溶解度 DMSO : 12.5 mg/mL (29.04 mM; ultrasonic and warming and heat to 60°C) 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 2.3232 mL 11.6158 mL 23.2315 mL
5 mM 0.4646 mL 2.3232 mL 4.6463 mL
10 mM 0.2323 mL 1.1616 mL 2.3232 mL
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Research Update

Fluorescence characteristics of 5-Carboxytetramethylrhodamine linked covalently to the 5' end of oligonucleotides: multiple conformers of single-stranded and double-stranded dye-DNA complexes

Biophys J 1996 Aug;71(2):972-94.PMID:8842236DOI:10.1016/S0006-3495(96)79300-1.

Fluorescence steady-state and lifetime experiments have been carried out on duplex and single-stranded DNA molecules labeled at the 5' ends with 5-Carboxytetramethylrhodamine (TMRh). The temperature and ionic strength of the solutions were varied over large ranges. The results reveal at least three well-defined states of the TMRh-DNA molecules for the single-stranded as well as for the double-stranded DNA molecules. Two states are fluorescent, with lifetimes in the range of 0.5-1 ns and 2.5-3 ns. A third state of TMRh-DNA does not fluoresce (a dark species of TMRh-DNA). The distribution of the TMRh-DNA molecules among these three states is strongly temperature and ionic strength dependent. Estimates are made of some reaction parameters of the multistate model. The results are discussed in terms of the photophysics of TMRh, and consequences of the multiple conformers of TMRh-DNA for studies involving fluorescence studies with TMRh-labeled DNA are considered.

Sequential Ag+/biothiol and synchronous Ag+/Hg2+ biosensing with zwitterionic Cu2+-based metal-organic frameworks

Analyst 2020 Apr 7;145(7):2779-2788.PMID:32101233DOI:10.1039/d0an00002g.

Zwitterionic metal-organic frameworks (MOFs) of {[Cu(Cbdcp)(Dps)(H2O)3]·6H2O}n (MOF 1) and [Cu4(Dcbb)4(Dps)2(H2O)2]n (MOF 2) (H3CbdcpBr = N-(4-carboxybenzyl)-(3,5-dicarboxyl)pyridinium bromide; H2DcbbBr = 1-(3,5-dicarboxybenzyl)-4,4'-bipyridinium bromide; Dps = 4,4'-dipyridyl sulfide) quench the fluorescence of cytosine-rich DNA tagged with 5-Carboxytetramethylrhodamine (TAMRA, emission at 582 nm, denoted as C-rich P-DNA-1) and yield the corresponding P-DNA-1@MOF hybrids. Exposure of these hybrids to Ag+ results in the release of the P-DNA-1 strands from the MOF surfaces as double-stranded, hairpin-like C-AgI-C (ds-DNA-1@Ag+) with the restoration of TAMRA fluorescence. The ds-DNA-1@Ag+ formed on the surface of 1 can subsequently sense biothiols cysteine (Cys), glutathione (GSH), and homocysteine (Hcy) due to the stronger affinity of mercapto groups for Ag+ that serves to unfold the ds-DNA-1@Ag+ duplex, reforming P-DNA-1, which is re-adsorbed by MOF 1 accompanied by quenching of TAMRA emission. Meanwhile, MOF 2 is also capable of co-loading a thymine-rich probe DNA tagged with 5-carboxyfluorescein (FAM, emission at 518 nm, denoted as T-rich P-DNA-2) to achieve synchronous sensing of Ag+ and Hg2+, resulting from the simultaneous yet specific ds-DNA-1@Ag+ and T-HgII-T duplex (ds-DNA-2@Hg2+) formation, as well as the distinctive emission wavelengths of TAMRA and FAM. Detection limits are as low as 5.3 nM (Ag+), 14.2 nM (Cys), 13.5 nM (GSH), and 9.1 nM (Hcy) for MOF 1, and 7.5 nM (Ag+) and 2.6 nM (Hg2+) for MOF 2, respectively. The sequential sensing of Ag+ and biothiols by MOF 1, and the synchronous sensing of Ag+ and Hg2+ by MOF 2 are rapid and specific, even in the presence of other mono- and divalent metal cations or other biothiols at much higher concentrations. Molecular simulation studies provide insights regarding the molecular interactions that underpin these sensing processes.

Immunoassay for rapid on-site detection of glyphosate herbicide

Environ Monit Assess 2019 Jul 24;191(8):507.PMID:31342281DOI:10.1007/s10661-019-7657-z.

Glyphosate is the most widespread herbicide and its global use is steadily increasing. Although glyphosate is considered to have low toxicity, its wide application has raised concerns about its effects on human health. The extensive use of glyphosate has risen a need of its continuous monitoring in drinking and surface waters to assure in accordance with the set standards. Within the present study, we have developed a novel assay for the on-site detection of glyphosate by combining flow-through technology with the high specificity of immunorecognition. The proposed biosensing system was based on the detection of fluorescence signal generated by the quantitative replacement of glyphosate in antigen-antibody complex with IgY-type anti-glyphosate antibodies on microbeads by synthetic 5-Carboxytetramethylrhodamine (5-TAMRA) conjugated glyphosate. The working range of this assay was in low millimolar range and the time required for glyphosate detection around 0.5 h. The applicability of the immunoassay for glyphosate detection in surface water was tested and the biosensor results were validated with high-performance liquid chromatography.

A novel photosensitizer for light-controlled gene silencing

Nucleic Acid Ther 2011 Oct;21(5):359-67.PMID:22004417DOI:10.1089/nat.2011.0309.

We here demonstrate for the first time that 5-Carboxytetramethylrhodamine (TAMRA) covalently linked to nuclear localization signal (NLS)-conjugated peptide nucleic acids (PNAs) are photosensitizers (PSs) with the capacity to initiate photochemical damage to endocytic membranes, resulting in release of endocytosed material into cytosol. Our results show that TAMRA/PNA/NLS conjugates work as multifunctional molecules by offering cellular uptake, PNA-directed gene silencing, and the possibility for targeting in a light-controlled manner. In addition to PNA-directed gene silencing, we demonstrate that TAMRA/PNA/NLS molecules may function as a PS for light-controlled release of small interfering RNA molecules from the endocytic pathway when combined with an appropriate carrier. Using these strategies, we could silence the S100A4 gene at both protein and mRNA levels in a light-controlled manner, without any detectable reduction in cell viability. Our data demonstrate the possibility for light-controlled delivery of macromolecules entrapped within endocytic vesicles using multifunctional TAMRA/PNA/NLS molecules as PSs.

The Chemerin Receptor CMKLR1 Requires Full-Length Chemerin for High Affinity in Contrast to GPR1 as Demonstrated by a New Nanoluciferase-Based Binding Assay

ChemMedChem 2022 Dec 5;17(23):e202200413.PMID:36178206DOI:10.1002/cmdc.202200413.

To study the binding mode of the adipokine chemerin as well as the short peptide agonist chemerin-9 (C9) to its two receptors chemokine-like receptor 1 (CMKLR1) and G protein-coupled receptor 1 (GPR1), we generated 5-Carboxytetramethylrhodamine (TAMRA) modified variants of both ligands. In addition, we labeled GPR1 and CMKLR1 with a nanoluciferase at the N-terminus to perform NanoBRET binding assays. For GPR1, both ligands show high affinity and comparable binding. Significant differences were found for CMKLR1, whereby only full-length chemerin binds with high affinity in saturation and displacement assays. For TAMRA-C9 a biphasic binding consisting of two binding states has been found and no displacement studies could be performed. Thus, we conclude that CMKLR1 requires full-length chemerin for stable binding in contrast to GPR1. This work demonstrates the NanoBRET binding assay as a new tool for binding studies at chemerin receptors and it enables deeper insights into the ligand binding parameters.