Octadecyl Rhodamine B Chloride (R18)
Octadecyl Rhodamine B Chloride (R18)
Invitrogen™

Octadecyl Rhodamine B Chloride (R18)

The lipophilic octadecyl rhodamine B binds to membranes with the fluorophore at the aqueous interface and the alkyl tail protrudingLeia mais
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Número do catálogoQuantity
O24610 mg
Número do catálogo O246
Preço (BRL)
3.406,76
Each
Adicionar ao carrinho
Quantity:
10 mg
Preço (BRL)
3.406,76
Each
Adicionar ao carrinho
The lipophilic octadecyl rhodamine B binds to membranes with the fluorophore at the aqueous interface and the alkyl tail protruding into the lipid interior.
For Research Use Only. Not for use in diagnostic procedures.
Especificações
Molecular FormulaC46H67ClN2O3
Product LineMolecular Probes
Quantity10 mg
Recommended StorageStore in freezer (-5°C to -30°C) and protect from light.
Shipping ConditionRoom Temperature
Sub Cellular LocalizationCell Membranes & Lipids
Physical FormSolid
Product TypeCell Labeling Reagent
Unit SizeEach

Citações e referências (236)

Citações e referências
Abstract
Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.
Authors:Kozerski C,Ponimaskin E,Schroth-Diez B,Schmidt MF,Herrmann A
Journal:Journal of virology
PubMed ID:10906206
The fusion activity of chimeras of influenza virus hemagglutinin (HA) (from A/fpv/Rostock/34; subtype H7) with the transmembrane domain (TM) and/or cytoplasmic tail (CT) either from the nonviral, nonfusogenic T-cell surface protein CD4 or from the fusogenic Sendai virus F-protein was studied. Wild-type or chimeric HA was expressed in CV-1 cells ... More
Fusion activity of transmembrane and cytoplasmic domain chimeras of the influenza virus glycoprotein hemagglutinin.
Authors:Schroth-Diez B, Ponimaskin E, Reverey H, Schmidt MF, Herrmann A
Journal:J Virol
PubMed ID:9420208
The role of the sequence of transmembrane and cytoplasmic/intraviral domains of influenza virus hemagglutinin (HA, subtype H7) for HA-mediated membrane fusion was explored. To analyze the influence of the two domains on the fusogenic properties of HA, we designed HA-chimeras in which the cytoplasmic tail and/or transmembrane domain of HA ... More
Exocytotic insertion of calcium channels constrains compensatory endocytosis to sites of exocytosis.
Authors:Smith RM, Baibakov B, Ikebuchi Y, White BH, Lambert NA, Kaczmarek LK, Vogel SS
Journal:J Cell Biol
PubMed ID:10684256
'Proteins inserted into the cell surface by exocytosis are thought to be retrieved by compensatory endocytosis, suggesting that retrieval requires granule proteins. In sea urchin eggs, calcium influx through P-type calcium channels is required for retrieval, and the large size of sea urchin secretory granules permits the direct observation of ... More
Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.
Authors:Jain S, McGinnes LW, Morrison TG
Journal:J Virol
PubMed ID:17151113
'Newcastle disease virus (NDV), an avian paramyxovirus, initiates infection with attachment of the viral hemagglutinin-neuraminidase (HN) protein to sialic acid-containing receptors, followed by fusion of viral and cell membranes, which is mediated by the fusion (F) protein. Like all class 1 viral fusion proteins, the paramyxovirus F protein is thought ... More
Mild proteolysis induces a ready-to-fuse state on Sendai virus envelope.
Authors:Tomasi M, Baiocchi M, Moscufo N, Parolini I, Squatriti T, Bellini T, Dallocchio F
Journal:FEBS Lett
PubMed ID:9515725
'The Sendai virus fuses with host cell membranes in a pH-independent manner through an unknown mechanism. Here we report that mild trypsin pre-treatments of Sendai virions, for example 15 min at 4 degrees C, give Sendai virions the ability to fuse at a rate up to 10-fold higher than control. ... More