PBFI, AM, cell permeant - Special Packaging
PBFI, AM, cell permeant - Special Packaging
Invitrogen™

PBFI, AM, cell permeant - Special Packaging

PBFI is a potassium-sensitive molecule used measure intracellular K+ fluxes in animal cells and in plant cells and vacuoles. AlthoughRead more
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Catalog NumberQuantity
P1267MP20 x 50 μg
Catalog number P1267MP
Price (KRW)
1,043,000
온라인 행사
Ends: 31-Dec-2025
1,226,000
Save 183,000 (15%)
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Quantity:
20 x 50 μg
Price (KRW)
1,043,000
온라인 행사
Ends: 31-Dec-2025
1,226,000
Save 183,000 (15%)
Each
Add to cart
PBFI is a potassium-sensitive molecule used measure intracellular K+ fluxes in animal cells and in plant cells and vacuoles. Although the selectivity of PBFI for K+ is less than that of calcium indicators such as fura-2, it is sufficient for the detection of physiological concentrations of K+ in the presence of other monovalent cations. The spectral response of PBFI upon ion binding permit excitation ratio measurements, and this indicator can be used with the same optical filters and equipment used for fura-2.

Learn more about ion indicators including calcium, potassium, pH, and membrane potential indicators ›

Fluorescent Ion Indicators Specifications:
• Label (Ex/Em): PBFI (∼340,380/500 nm)
• Lyophilized product may be dissolved in DMSO for use
• Product is typically loaded into cells by adding the dissolved indicator to medium containing cells


Selectivity Considerations and Cell Loading Strategies
The Kd of PBFI for K+ is strongly dependent on whether Na+ is present, with a value of 5.1 mM in the absence of Na+ and 44 mM in solutions with a combined Na+ and K+ concentration of 135 mM (which approximates physiological ionic strength). In buffers in which the Na+ is replaced by tetramethylammonium chloride, the Kd of PBFI for K+ is 11 mM; choline chloride and N-methylglucamine are two other possible replacements for Na+ in the medium. Although PBFI is only 1.5-fold more selective for K+ than for Na+, this selectivity is often sufficient because intracellular K+ concentrations are normally about 10 times higher than Na+ concentrations.

PBFI is available as both cell-impermeant acid salt (P1265MP) and as cell-permeant acetoxymethyl (AM) esters (P1267MP). The anionic acid forms can be loaded into cells using our Influx™ pinocytic cell-loading reagent (I14402, Chelators, Calibration Buffers, Ionophores and Cell-Loading Reagents—Section 19.8), or by microinjection, patch-pipette infusion or electroporation. For AM ester loading (Loading and Calibration of Intracellular Ion Indicators—Note 19.1), addition of the Pluronic™ F-127 (P3000MP, P6866, P6867) or PowerLoad™ (P10020) dispersing agents as well as relatively long incubation times—up to four hours—are typically necessary.

Find Fluorescent Indicators for Na+ and K+
We offer a number of fluorescent indicators for measuring Na+ and K+. Review Fluorescent Na+ and K+ Indicators—Section 21.1 in the Molecular Probes™ Handbook for more information on these products.

For Research Use. Not for human or animal therapeutic or diagnostic use.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodFluorescence
Dye TypePotassium Indicator
Quantity20 x 50 μg
Shipping ConditionRoom Temperature
For Use With (Application)Cell Viability and Proliferation
For Use With (Equipment)Fluorescence Microscope
Product TypePBFI AM
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C and protect from light.

Citations & References (52)

Citations & References
Abstract
4-aminopyridine decreases progesterone production by porcine granulosa cells.
Authors:Li Y, Ganta S, von Stein FB, Mason DE, Mitchell BM, Freeman LC
Journal:Reprod Biol Endocrinol
PubMed ID:12740033
'BACKGROUND: Ion channels occur as large families of related genes with cell-specific expression patterns. Granulosa cells have been shown to express voltage-gated potassium channels from more than one family. The purpose of this study was to determine the effects of 4-aminopyridine (4-AP), an antagonist of KCNA but not KCNQ channels. ... More
Protein kinase G activation of K(ATP) channels in human-cultured prostatic stromal cells.
Authors:Cook AL, Frydenberg M, Haynes JM
Journal:Cell Signal
PubMed ID:12359308
'In this study, we identify and investigate the role of protein kinase G (PKG) in cells cultured from human prostatic stroma. Cells were used for immunocytochemistry, contractility or K(+) fluorescent imaging studies. All cultured prostatic stromal cells showed PKG immunostaining. Phorbol 12,13 diacetate (PDA, 1 microM) elicited contractions from human-cultured ... More
N-methyl-D-aspartate excitotoxicity: relationships among plasma membrane potential, Na(+)/Ca(2+) exchange, mitochondrial Ca(2+) overload, and cytoplasmic concentrations of Ca(2+), H(+), and K(+).
Authors:Kiedrowski L
Journal:Mol Pharmacol
PubMed ID:10462550
'A high cytoplasmic Na(+) concentration may contribute to N-methyl-D-aspartate (NMDA)-induced excitotoxicity by promoting Ca(2+) influx via reverse operation of the Na(+)/Ca(2+) exchanger (NaCaX), but may simultaneously decrease the electrochemical Ca(2+) driving force by depolarizing the plasma membrane (PM). Digital fluorescence microscopy was used to compare the effects of Na(+) versus ... More
Determination of the physical environment within the Chlamydia trachomatis inclusion using ion-selective ratiometric probes.
Authors:Grieshaber S, Swanson JA, Hackstadt T
Journal:Cell Microbiol
PubMed ID:12027956
'Chlamydia trachomatis is an obligate intracellular bacterium with a biphasic life cycle that takes place entirely within a membrane-bound vacuole termed an inclusion. The chlamydial inclusion is non-fusogenic with endosomal or lysosomal compartments but intersects a pathway involved in transport of sphingomyelin from the Golgi apparatus to the plasma membrane. ... More
Dynamics and consequences of potassium shifts in skeletal muscle and heart during exercise.
Authors:Sejersted OM, Sjøgaard G
Journal:Physiol Rev
PubMed ID:11015618
'Since it became clear that K(+) shifts with exercise are extensive and can cause more than a doubling of the extracellular [K(+)] ([K(+)](s)) as reviewed here, it has been suggested that these shifts may cause fatigue through the effect on muscle excitability and action potentials (AP). The cause of the ... More