Cholera Toxin Subunit B (Recombinant), Alexa Fluor™ 594 Conjugate
Cholera Toxin Subunit B (Recombinant), Alexa Fluor™ 594 Conjugate
Invitrogen™

Cholera Toxin Subunit B (Recombinant), Alexa Fluor™ 594 Conjugate

Molecular Probes™ cholera toxin conjugates are made from a recombinant version of the B subunit only. This allows us toRead more
Have Questions?
Change viewbuttonViewtableView
Catalog NumberQuantity
C22842500 μg
C34777100 μg
Catalog number C22842
Price (CLP)
1.026.326
Each
Add to cart
Quantity:
500 μg
Price (CLP)
1.026.326
Each
Add to cart
Molecular Probes™ cholera toxin conjugates are made from a recombinant version of the B subunit only. This allows us to provide a very high-purity product that is completely free of the toxic A subunit. Cholera toxin B subunit (CT-B) attaches to cells by binding to ganglioside GM1, making it a powerful tool for retrograde labeling of neurons. This tracer has been used in a variety of applications, including tracing of rat forebrain afferents, projections of the parabrachial region, and neurons of the urinary bladder wall. When used in neuronal tracing applications, CT-B is typically introduced by pressure injection or by iontophoretic injection into neural tissue.

Cholera Toxin Subunit B Specifications:
• Label (Ex/Em): Alexa Fluor™ 594 (590/617 nm)
• At neutral pH, the 11.4 kDa B subunit exists as a 57 kDa pentamer
• Lyophilized product can be dissolved in buffer (e.g., PBS) for use


Cholera Toxin Subunit B for Studying Lipid Rafts
More recently, researchers have found that CT-B can be used as a marker for lipid rafts, which are membrane microdomains enriched in cholesterol and sphingolipids thought to be important in cell signaling. For lipid raft staining, cells are first incubated with fluorescent CT-B. Then, an anti–CT-B antibody is added to crosslink the CT-B in the lipid rafts into distinct patches on the plasma membrane. These patches are easily visualized by fluorescence microscopy. In addition to individual fluorescent CT-B conjugates, we also offer Vybrant™ Lipid Raft Labeling Kits that contain the Alexa Fluor™ 488, Alexa Fluor™ 555, or Alexa Fluor™ 594 dye conjugates of CT-B, an anti–CT-B antibody, and a detailed protocol for labeling and preparing cells for fluorescence microscopy.

Find More CT-B Conjugates
We offer various CT-B conjugates. Review Protein Conjugates—Section 14.7 in the Molecular Probes™ Handbook for more information on these tracers.

For Research Use Only. Not for human or animal therapeutic or diagnostic use.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Label TypeAlexa Fluor Dyes
Product LineAlexa Fluor
Protein FormRecombinant
Protein SubtypeCholera Toxin
Quantity500 μg
Shipping ConditionRoom Temperature
ConjugateAlexa Fluor 594
FormLyophilized
RecombinantRecombinant
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C) and protect from light.

Citations & References (35)

Citations & References
Abstract
Chondrocytes utilize a cholesterol-dependent lipid translocator to externalize phosphatidylserine.
Authors:Damek-Poprawa M, Golub E, Otis L, Harrison G, Phillips C, Boesze-Battaglia K
Journal:Biochemistry
PubMed ID:16519527
'During endochondral ossification, growth plate chondrocytes release plasma membrane (PM) derived matrix vesicles (MV), which are the site of initial hydroxyapatite crystal formation. MV constituents which facilitate the mineralization process include the integral membrane ectoenzymes alkaline phosphatase (ALPase) and nucleotide pyrophosphatase phosphodiesterase (NPP1/PC-1), along with a phosphatidylserine- (PS-) rich membrane ... More
Inhibition of caveolar uptake, SV40 infection, and beta1-integrin signaling by a nonnatural glycosphingolipid stereoisomer.
Authors:Singh RD, Holicky EL, Cheng ZJ, Kim SY, Wheatley CL, Marks DL, Bittman R, Pagano RE
Journal:J Cell Biol
PubMed ID:17371832
'Caveolar endocytosis is an important mechanism for the uptake of certain pathogens and toxins and also plays a role in the internalization of some plasma membrane (PM) lipids and proteins. However, the regulation of caveolar endocytosis is not well understood. We previously demonstrated that caveolar endocytosis and beta1-integrin signaling are ... More
Gbetagamma activation of Src induces caveolae-mediated endocytosis in endothelial cells.
Authors:Shajahan AN, Tiruppathi C, Smrcka AV, Malik AB, Minshall RD,
Journal:J Biol Chem
PubMed ID:15345719
'Caveolae-mediated endocytosis in endothelial cells is stimulated by the binding of albumin to gp60, a specific albumin-binding protein localized in caveolae. The activation of gp60 induces its cell surface clustering and association with caveolin-1, the caveolar-scaffolding protein. This interaction leads to G(i)-induced Src kinase activation, which in turn signals dynamin-2-mediated ... More
Plasticity of B cell receptor internalization upon conditional depletion of clathrin.
Authors:Stoddart A, Jackson AP, Brodsky FM
Journal:Mol Biol Cell
PubMed ID:15716350
'B cell antigen receptor (BCR) association with lipid rafts, the actin cytoskeleton, and clathrin-coated pits influences B cell signaling and antigen presentation. Although all three cellular structures have been separately implicated in BCR internalization, the relationship between them has not been clearly defined. In this study, internalization pathways were characterized ... More
Condensed complexes, rafts, and the chemical activity of cholesterol in membranes.
Authors:Radhakrishnan A, Anderson TG, McConnell HM
Journal:Proc Natl Acad Sci U S A
PubMed ID:11050164
'Epifluorescence microscopy studies of mixtures of phospholipids and cholesterol at the air-water interface often exhibit coexisting liquid phases. The properties of these liquids point to the formation of "condensed complexes" between cholesterol and certain phospholipids, such as sphingomyelin. It is found that monolayers that form complexes can incorporate a low ... More