BAPTA, Tetracesium Salt, cell impermeant

BAPTA es un quelante altamente selectivo para Ca2+ sobre Mg2+ y puede usarse para controlar el nivel de Ca2+ extracelular.Más información

Número de catálogo	Cantidad
B1212	1 g

Número de catálogo B1212

Precio (MXN)

Cantidad:

BAPTA es un quelante altamente selectivo para Ca²⁺ sobre Mg²⁺ y puede usarse para controlar el nivel de Ca²⁺ extracelular. BAPTA es más selectivo para Ca²⁺ que EDTA y EGTA, y su unión al metal es también menos sensible al pH.

Obtenga más información sobre los indicadores de iones, incluidos los indicadores de calcio, potasio, pH y potencial de la membrana ›

Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.

Especificaciones

Tipo de coloranteQuelante (no fluorescente)

Cantidad1 g

Condiciones de envíoTemperatura ambiente

Tipo de productoViabilidad y proliferación celulares

Unit SizeEach

Contenido y almacenamiento

Almacenar a temperatura ambiente.

Citations & References (22)

Citations & References

Abstract

Neurosteroids modulate calcium currents in hippocampal CA1 neurons via a pertussis toxin-sensitive G-protein-coupled mechanism.

Authors:ffrench-Mullen JM, Danks P, Spence KT

Journal:J Neurosci

PubMed ID:8158251

'The inhibition of Ca2+ channel currents by endogenous brain steroids was examined in freshly dissociated pyramidal neurons from the adult guinea pig hippocampal CA1 region. The steady-state inhibition of the peak Ca2+ channel current evoked by depolarizing steps from -80 to -10 mV occurred in a concentration-dependent manner with the ... More

Calcium-induced inactivation of NMDA receptor-channels evolves independently of run-down in cultured rat brain neurones.

Authors:Medina I, Filippova N, Bakhramov A, Bregestovski P

Journal:J Physiol

PubMed ID:8887753

'1. Calcium-induced transient inactivation of NMDA receptor (NMDAR) channels was studied in cultured rat hippocampal and cerebellar granule neurones using patch-clamp techniques and confocal scanning microscopy. 2. During whole-cell recordings, in the presence of 2 mM external Ca2+, conditioning (2-20 s) pulses of NMDA (20-100 microM) caused a transient decrease ... More

A store-operated calcium channel in Drosophila S2 cells.

Authors:Yeromin AV, Roos J, Stauderman KA, Cahalan MD

Journal:J Gen Physiol

PubMed ID:14744989

'Using whole-cell recording in Drosophila S2 cells, we characterized a Ca(2+)-selective current that is activated by depletion of intracellular Ca2+ stores. Passive store depletion with a Ca(2+)-free pipette solution containing 12 mM BAPTA activated an inwardly rectifying Ca2+ current with a reversal potential >60 mV. Inward currents developed with a ... More

Ca2+ store dynamics determines the pattern of activation of the store-operated Ca2+ current I(CRAC) in response to InsP3 in rat basophilic leukaemia cells.

Authors:Glitsch MD, Parekh AB

Journal:J Physiol

PubMed ID:10699074

'1. The relationship between the amplitude of the store-operated Ca2+ ICR AC and intracellular inositol 1,4,5-triphosphate (InsP3) concentration is complex. In rat basophilic leukaemia (RBL-1) cells dialysed with high intracellular Ca2+ buffer, the relationship is supra-linear with a Hill coefficient of 12 and resembles an apparent ''all-or-none'' phenomenon. The non-linearity ... More

Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses.

Authors:Lonart G, Schoch S, Kaeser PS, Larkin CJ, Südhof TC, Linden DJ

Journal:Cell

PubMed ID:14532002

'Presynaptic activation of protein kinase A (PKA) induces LTP in cerebellar parallel fiber synapses. Presynaptic LTP is known to require the active zone protein RIM1alpha, but the underlying induction mechanism remains unclear. We now show that PKA directly phosphorylates RIM1alpha at two sites. Using paired recordings from cultured cerebellar granule ... More

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