BAPTA, Tetracesium Salt, cell impermeant
BAPTA, Tetracesium Salt, cell impermeant
Invitrogen™

BAPTA, Tetracesium Salt, cell impermeant

BAPTA is a cell-impermeant chelator, which is a highly selective for Ca2+ over Mg2+, and it can be used toRead more
Have Questions?
Catalog NumberQuantity
B12121 g
Catalog number B1212
Price (CNY)
6,228.00
Each
Add to cart
Quantity:
1 g
Price (CNY)
6,228.00
Each
Add to cart
BAPTA is a cell-impermeant chelator, which is a highly selective for Ca2+ over Mg2+, and it can be used to control the level of extracellular Ca2+. BAPTA is more selective for Ca2+ than EDTA and EGTA, and its metal binding is also less sensitive to pH.

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

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Dye TypeChelator (Non-Fluorescent)
Quantity1 g
Shipping ConditionRoom Temperature
Product TypeCell-Impermeant Chelator
Unit SizeEach
Contents & Storage
Store at room temperature.

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