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Sulforhodamine B acid chloride Sale

(Synonyms: 丽丝胺碱性蕊香红B磺酰氯) 目录号 : GC30195

SulforhodamineBacidchloride是形成稳定共轭物的荧光蛋白标记物.

Sulforhodamine B acid chloride Chemical Structure

Cas No.:62796-29-6

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100mg
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产品描述

Sulforhodamine B acid chloride is a fluorescent protein label forming stable conjugates.

Sulforhodamine B (SRB) is often used as a membrane-impermeable polar tracer or used for cell density determination via determination of cellular proteins (cytotoxicity assay). The SRB assay has been used to inexpensively conduct various screening assays to investigate cytotoxicity in cell based studies. This method relies on the property of SRB, which binds stoichiometrically to proteins under mild acidic conditions and then can be extracted using basic conditions; thus, the amount of bound dye can be used as a proxy for cell mass, which can then be extrapolated to measure cell proliferation. The protocol can be divided into four main steps: preparation of treatment, incubation of cells with treatment of choice, cell fixation and SRB staining, and absorbance measurement. This assay is limited to manual or semiautomatic screening, and can be used in an efficient and sensitive manner to test chemotherapeutic drugs or small molecules in adherent cells. It also has applications in evaluating the effects of gene expression modulation (knockdown, gene expression upregulation), as well as to study the effects of miRNA replacement on cell proliferation[1].

[1]. Orellana EA, et al. Sulforhodamine B (SRB) Assay in Cell Culture to Investigate Cell Proliferation. Bio Protoc. 2016 Nov 5;6(21). pii: e1984.

Chemical Properties

Cas No. 62796-29-6 SDF
别名 丽丝胺碱性蕊香红B磺酰氯
Canonical SMILES CCN(C1=CC2=[O+]C3=C(C=CC(N(CC)CC)=C3)C(C4=CC=C(S(=O)(Cl)=O)C=C4S(=O)([O-])=O)=C2C=C1)CC
分子式 C27H29ClN2O6S2 分子量 577.11
溶解度 DMSO : ≥ 100 mg/mL (173.28 mM);Water : 10 mg/mL (17.33 mM) 储存条件 Store at -20°C
General tips 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液;一旦配成溶液,请分装保存,避免反复冻融造成的产品失效。
储备液的保存方式和期限:-80°C 储存时,请在 6 个月内使用,-20°C 储存时,请在 1 个月内使用。
为了提高溶解度,请将管子加热至37℃,然后在超声波浴中震荡一段时间。
Shipping Condition 评估样品解决方案:配备蓝冰进行发货。所有其他可用尺寸:配备RT,或根据请求配备蓝冰。

溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.7328 mL 8.6639 mL 17.3277 mL
5 mM 0.3466 mL 1.7328 mL 3.4655 mL
10 mM 0.1733 mL 0.8664 mL 1.7328 mL
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第一步:请输入基本实验信息(考虑到实验过程中的损耗,建议多配一只动物的药量)
给药剂量 mg/kg 动物平均体重 g 每只动物给药体积 ul 动物数量
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Research Update

Evaluation of fluorescent polysaccharide nanoparticles for pH-sensing

Org Biomol Chem.2009 May 7;7(9):1884-9.PMID:19590784DOI: 10.1039/b900260j.

The comprehensive characterization of novel dextran nanoparticles with regard to their suitability as pH-sensors for analytical applications (e.g. in physiology) is described. The nanoparticles are labeled with both a pH-indicator dye (fluorescein isothiocyanate, FITC) and a reference dye (sulforhodamine B acid chloride) as an internal standard. The fluorescence intensity of FITC increases with increasing pH, whereas the signal of the reference dye remains constant. Plotting the ratio of both signals against the pH gives a pK(a) of 6.45, which is appropriate for most of the measurement purposes. Furthermore, the influence of temperature, ionic strength and oxidizing substances on the performance of the fluorophores inside the dextran nanoparticles is examined. These results are compared to the dissolved dyes in order to evaluate if the dextran matrix affects the fluorescence properties of the sensor and the reference dye, and whether or not these nanosensors are suitable for pH-sensing in biological samples.

Fluorescent somatostatin receptor probes for the intraoperative detection of tumor tissue with long-wavelength visible light

Bioorg Med Chem.2002 Aug;10(8):2543-52.PMID:12057643DOI: 10.1016/s0968-0896(02)00114-1.

Targeted fluorescent dyes are of substantial value for the intraoperative delineation of primary tumors and metastatic lesions. For this purpose long-wavelength red light (lambda=550-650 nm) offers advantages because of good tissue penetration and direct visibility. Since somatostatin receptors (SSTR) are overexpressed in a number of tumors, a series of potentially tumor-selective peptide-dye conjugates were synthesized by solid-phase peptide synthesis (SPPS). The octapeptides octreotate, Tyr(3)-octreotate and Tyr(3)-octreotide were employed and exhibited high affinity for somatostatin receptors (SSTR). The fluorescent dyes rhodamine 101, sulforhodamine B acid chloride, sulforhodamine 101 or rhodamine B isothiocyanate were conjugated either directly or via spacers, for example the peptidase-labile pentapeptide sequence Ala-Leu-Ala-Leu-Ala. The conjugates were completely assembled on the solid support: Fmoc-SPPS, cyclization via a disulfide linkage, N-terminal attachment of a spacer, and linkage to the fluorescent dye. An in vitro competition assay revealed that the conjugates bind to SSTRs with IC(50) values between 0.7 and 89 nM. The conjugates were generally stable to hydrolysis at pH 7-8 in buffer or serum. However, the rhodamine 101 conjugates revealed a loss of absorption at alkaline pH due to conversion to a neutral spirolactam form, as characterized by NMR.

Cytotoxicity and antitumoral activity of dichloromethane extract and its fractions from Pothomorphe umbellata

Braz J Med Biol Res.2008 May;41(5):411-5.PMID:18545814DOI: 10.1590/s0100-879x2008000500010.

The cytotoxicity of the dichloromethane crude extract (DCE), obtained from the aerial parts of Pothomorphe umbellata (L.) Miq (Piperaceae), was evaluated against nine human cancer cell lines (MCF-7, NCI-ADR/RES, OVCAR-3, PC-3, HT-29, NCI-H460, 786-O, UACC-62, K-562). The DCE presented antiproliferative activity with good potency against all cell lines at low concentrations (between 4.0 and 9.5 microg/mL) and with selectivity (1.55 microg/mL) for the leukemia cell line (K-652). DCE (100, 200, 300 and 400 mg/kg, ip) was also evaluated in the Ehrlich ascites tumor model. Both the survival number and the life span of the animals that died increased by at least 45 and 50%, respectively (8 animals per group), demonstrating P. umbellata extract potential anticancer activity. The results of the in vivo antitumor activity prompted the fractionation of the crude extract. The crude extract was submitted to dry column chromatography with dichloromethane-methanol (99:1). The column effluent fractions were extracted with methanol, dried under vacuum yielding fractions FR1 (less polar), FR2 (medium polarity), and FR3 (polar), which were analyzed for their growth inhibition or cytotoxic properties by a 48-h sulforhodamine B cell viability assay by measuring the total protein content. FR1 demonstrated high potency and cytotoxicity, a result compatible with the high toxicity of oxalic acid; FR2, containing 4-nerolidylcathecol, presented the lowest cytotoxic activity compared to the other two fractions but with selectivity for prostate cancer cell line; FR3, containing a mixture of steroids described in the literature as possessing various biological activities, also presented potent anticancer in vitro activity. These results suggest that P. umbellata DCE in vivo antitumor activity may be a consequence of the activity of different active principles.

Preparation of functional aptamer films using layer-by-layer self-assembly

Biomacromolecules.2009 May 11;10(5):1149-54.PMID:19385646DOI: 10.1021/bm8014126.

Advances in many aptamer-based applications will require a better understanding of how an aptamer's molecular recognition ability is affected by its incorporation into a suitable matrix. In this study, we investigated whether a model aptamer system, the sulforhodamine B aptamer, would retain its binding ability while embedded in a multilayer polyelectrolyte film. Thin films consisting of poly(diallyldimethylammonium chloride) as the polycation and both poly(sodium 4-styrene-sulfonate) and the aptamer as the polyanions were deposited by the layer-by-layer approach and were compared to films prepared using calf thymus DNA or a random single-stranded oligonucleotide. Data from UV-vis spectroscopy, quartz crystal microbalance studies, confocal microscopy, and time of flight secondary ion mass spectrometry confirm that the aptamer's recognition of its target is retained, with no loss of specificity and only a modest reduction of binding affinity, while it is incorporated within the thin film. These findings open up a raft of new opportunities for the development and application of aptamer-based functional thin films.

Vacuole formation in fatigued skeletal muscle fibres from frog and mouse: effects of extracellular lactate

J Physiol.2000 Aug 1;526 Pt 3(Pt 3):597-611.PMID:10922011DOI: 10.1111/j.1469-7793.2000.00597.x.

Isolated, living muscle fibres from either Xenopus or mouse were observed in a confocal microscope and t-tubules were visualized with sulforhodamine B. Observations were made before and after fatiguing stimulation. In addition, experiments were performed on fibres observed in an ordinary light microscope with dark-field illumination. In Xenopus fibres, recovering after fatigue, t-tubules started to show dilatations 2-5 min post-fatigue. These swellings increased in size over the next 10-20 min to form vacuoles. After 2-3 h of recovery the appearance of the fibres was again normal and force production, which had been markedly depressed 10-40 min post-fatigue, was close to control. Vacuoles were not observed in mouse fibres, fatigued with the same protocol and allowed to recover. In Xenopus fibres, fatigued in normal Ringer solution and allowed to recover in Ringer solution with 30-50 mM L-lactate substituting for chloride (lactate-Ringer), the number and size of vacuoles were markedly reduced. Also, force recovery was significantly faster. Replacement of chloride by methyl sulphate or glucuronate had no effect on vacuolation. Resting Xenopus fibres exposed to 50 mM lactate-Ringer and transferred to normal Ringer solution displayed vacuoles within 5-10 min, but to a smaller extent than after fatigue. Vacuolation was not associated with marked force reduction. Mouse fibres, fatigued in 50 mM lactate-Tyrode (L-lactate substituting for chloride in Tyrode solution) and recovering in normal Tyrode solution, displayed vacuoles for a limited period post-fatigue. Vacuolation had no effect on force production. The results are consistent with the view that lactate, formed during fatigue, is transported into the t-tubules where it attracts water and causes t-tubule swelling and vacuolation. This vacuolation may be counteracted in vivo due to a gradual extracellular accumulation of lactate during fatigue.