5.05766
Casein Kinase II Inhibitor XII, TBBz
Synonym(e):
Casein Kinase II Inhibitor XII, TBBz, 4,5,6,7-Tetrabromobenzimidazole, CYP24A1 inhibitor, TBBz, CK2 Inhibitor, TBBz
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Alle Fotos(1)
About This Item
Empirische Formel (Hill-System):
C7H2Br4N2
CAS-Nummer:
Molekulargewicht:
433.72
MDL-Nummer:
UNSPSC-Code:
12352200
Empfohlene Produkte
Assay
≥99% (HPLC)
Qualitätsniveau
Form
powder
Wirksamkeit
70 nM Ki
Hersteller/Markenname
Calbiochem®
Lagerbedingungen
OK to freeze
protect from light
Farbe
off-white
Löslichkeit
DMSO: 100 mg/mL
Lagertemp.
2-8°C
InChI
1S/C7H2Br4N2/c8-2-3(9)5(11)7-6(4(2)10)12-1-13-7/h1H,(H,12,13)
InChIKey
LOEIRDBRYBHAJB-UHFFFAOYSA-N
Allgemeine Beschreibung
A cell-permeable halogenated benzimidazole compound that acts as a selective and ATP competitive inhibitor of casein kinase II (CK2, Ki = 70 nM for the active hetero-tetrameric form). However, its effect on free CK2a and CK2a′ subunits is significantly reduced (Ki = 510 and 400 nM, respectively). Reported to reduce viability and proliferation in HeLa, Jurkat, and HL-60 cells (at ˜25 µM). Also shown to disrupt the promoter activity of CYP24A1 and down-regulates its endogenous and 1, 25-Vitamin D3 (1,25-D3)-induced expression in PC3 cells. Synergistically enhances the anti-tumor effect of 1, 25-D3 in a PC3 xenograft murine model.
Biochem./physiol. Wirkung
Primary Target
CK2
CK2
Reversible: yes
Verpackung
Packaged under inert gas
Warnhinweis
Toxicity: Standard Handling (A)
Rekonstituierung
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Sonstige Hinweise
Szyszka, R. et al. 1995. Biochem. Biophys. Res. Comm.208, 418.
Zien, P. et al. 2003. Biochem. Biophys. Res. Comm.306, 129.
Zien, P. et al. 2003. Biochem. Biophys. Res. Comm.312, 623.
Zien, P. et al. 2005. Biochim. Biophy. Acta1754, 271.
Luo, W. et al. 2013. Cancer Res.73, 2289.
Zien, P. et al. 2003. Biochem. Biophys. Res. Comm.306, 129.
Zien, P. et al. 2003. Biochem. Biophys. Res. Comm.312, 623.
Zien, P. et al. 2005. Biochim. Biophy. Acta1754, 271.
Luo, W. et al. 2013. Cancer Res.73, 2289.
Rechtliche Hinweise
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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Piotr Zień et al.
Biochemical and biophysical research communications, 312(3), 623-628 (2003-12-19)
Two ATP-competitive inhibitors-4,5,6,7-tetrabromo-benzotriazole (TBBt) and 4,5,6,7-tetrabromo-benzimidazole (TBBz) have been shown to decrease activity of CK2 holoenzyme. Surprisingly it occurs that TBBz contrary to TBBt does not inhibit free catalytic subunit CK2 [Formula: see text]. Both inhibitors are virtually inactive against
Piotr Zien et al.
Biochimica et biophysica acta, 1754(1-2), 271-280 (2005-10-06)
The development of selective cell-permeable inhibitors of protein kinase CK2 has represented an important advance in the field. However, it is important to not overlook the existence of discrete molecular forms of CK2 that arise from the presence of distinct
Wei Luo et al.
Cancer research, 73(7), 2289-2297 (2013-01-30)
Vitamin D has broad range of physiological functions and antitumor effects. 24-Hydroxylase, encoded by the CYP24A1 gene, is the key enzyme for degrading many forms of vitamin D including the most active form, 1,25D(3). Inhibition of CYP24A1 enhances 1,25D(3) antitumor
Piotr Zień et al.
Biochemical and biophysical research communications, 306(1), 129-133 (2003-06-06)
Like the previously reported 4,5,6,7-tetrabromobenzotriazole (TBBt), the structurally related 4,5,6,7-tetrabromobenzimidazole (TBBz) is a selective ATP-competitive inhibitor of protein kinase CK2 from such divergent sources as yeast, rat liver, Neurospora crassa and Candida tropicalis, with K(i) values in the range 0.5-1
R Szyszka et al.
Biochemical and biophysical research communications, 208(1), 418-424 (1995-03-08)
Several halogeno benzimidazole riboside inhibitors of animal and plant protein kinases CK I and CK II (also known as casein kinases I and II), were found to be effective inhibitors of Saccharomyces cerevisiae CK II, but not of the 27-kDa
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