MW 362.23 Da, Purity >98%. Potent and selective KCa1.1 channel activator. Induces a concentration-dependent decrease in mitochondrial membrane potential (EC50 = 3.6 μM).
(R)-limonene 6-monooxygenase, (S)-limonene 6-monooxygenase, (S)-limonene 7-monooxygenase, BK channel, BKCA alpha, BKCA alpha subunit, BKTM, CP2C9_HUMAN, CPC12, CPC8, CPC9, CPCJ, CYP2C, CYP2C10, CYPIIC9, Calcium-activated potassium channel, Calcium-activated potassium channel subunit alpha-1, Cytochrome P-450MP, Cytochrome P450 2C9, Cytochrome P450 MP-4, Cytochrome P450 MP-8, Cytochrome P450 PB-1, Cytochrome P450, family 2, subfamily C, polypeptide 9, Drosophila slowpoke like, HS90A_HUMAN, HSP 84, HSP 86, HSP 90, HSP 90 b, HSP90A, HSP90AA1, HSP90AB1, HSPC1, HSPC2, HSPCAL1, HSPCAL4, Heat shock 86 kDa, Heat shock protein 90kDa alpha cytosolic class A member 1, Heat shock protein 90kDa alpha cytosolic class B member 1, Heat shock protein HSP 90-alpha, Heat shock protein HSP 90-beta, K(VCA)alpha, KCMA1_HUMAN, KCNMA, KCNMA1, KCa1.1, MGC149605, MGC88320, Maxi K channel, Maxi Potassium channel alpha, MaxiK, Microsomal monooxygenase, OTTHUMP00000020135, P450 MP, P450 PB 1, P450C2C, P450IIC19, P450IIC9, Renal carcinoma antigen NY-REN-38, S-mephenytoin 4-hydroxylase, SAKCA, SLO, Slo homolog, Slo-alpha, Slo1, Slowpoke homolog, Xenobiotic monooxygenase, cytochrome P-450 S-mephenytoin 4-hydroxylase, flavoprotein-linked monooxygenase, hSlo, subfamily M subunit alpha-1
MW 362.23 Da, Purity >98%. Potent and selective KCa1.1 channel activator. Induces a concentration-dependent decrease in mitochondrial membrane potential (EC50 = 3.6 μM).
Soluble in ethanol to 100 mM.
Soluble in DMSO to 100 mM.
Potent and selective KCa1.1 channel activator. Induces a concentration-dependent decrease in mitochondrial membrane potential (EC50 = 3.6 μM).
Hsp90 also known as Heat Shock Protein 90 is a molecular chaperone with a mass of approximately 90 kDa. It plays a role in stabilizing and activating client proteins which are often involved in signal transduction. Hsp90 is found in the cytoplasm of eukaryotic cells and is highly expressed in response to stress. It is essential for maintaining cellular protein homeostasis under normal and stress conditions.
Hsp90 interacts with various client proteins to facilitate their correct folding maturation activation and stabilization. It is a part of a chaperone complex that includes co-chaperones such as Cdc37 and p23 which aid in its function. Hsp90 influences several cellular processes including cell cycle control and apoptosis. Its involvement in these processes makes it a critical player in cellular regulation and adaptation.
Hsp90 is integral to the MAPK and PI3K/AKT signaling pathways. It interacts with related proteins like Raf-1 and Akt ensuring their proper folding and function. Through these pathways Hsp90 supports cellular growth and survival playing a significant role in signal transduction and cellular response to external stimuli.
Hsp90 is often implicated in cancer and neurodegenerative diseases. Its overexpression is linked to cancer progression as it stabilizes several oncogenic client proteins like HER2. In neurodegenerative diseases Hsp90 interacts with proteins such as Tau and huntingtin; improper regulation can lead to disease progression. These associations highlight Hsp90's potential as a therapeutic target for various pathological conditions.
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NS-1619 blocks KCa1.1 currents in Xenopus oocytes. A. Families of KCa1.1 channel current responses to increasing voltage step stimulation (from -50 mV to + 50 mV), before (left) and during (right) application of 100 µM NS-1619 (ab141824). Currents were elicited by 100 ms voltage step from -100mV applied every 10 sec. B. Time course of current amplitude at 0 mV before, during application of 100 µM NS-1619 (green) and upon wash, demonstrating the current amplitude enhancement. C. Voltage dependence of KCa1.1 channel activity enhancement.
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