|Source:||From Streptomyces griseolavendus|
|Biological Activity or Inhibitors:||1. Lavendustin A and hormothamnione exhibit cytotoxic effects on tumor cell lines.
2. Lavendustin A is a potent tyrosine kinase inhibitor of the epidermal growth factor (EGF) receptor, and an angiogenesis inhibitor.
3. Lavendustin A is a hyperbolic mixed-type inhibitor with respect to both ATP and the peptide substrate, with a major effect on the binding affinities for both substrates.
4. Lavendustin A at 0.1 nM-1 microM causes a concave-shaped inhibition of the insulin release stimulated by 7 mM glucose, the inhibitory effect can be overcomed by higher concentrations of glucose.
|Solvent:||Chloroform, Dichloromethane, Ethyl Acetate, DMSO, Acetone, etc.|
|Storage:||Providing storage is as stated on the product vial and the vial is kept tightly sealed, the product can be stored for up to 24 months(2-8C).
Wherever possible, you should prepare and use solutions on the same day. However, if you need to make up stock solutions in advance, we recommend that you store the solution as aliquots in tightly sealed vials at -20C. Generally, these will be useable for up to two weeks. Before use, and prior to opening the vial we recommend that you allow your product to equilibrate to room temperature for at least 1 hour.
Need more advice on solubility, usage and handling? Please email to: firstname.lastname@example.org
|After receiving:||The packaging of the product may have turned upside down during transportation, resulting in the natural compounds adhering to the neck or cap of the vial. take the vial out of its packaging and gently shake to let the compounds fall to the bottom of the vial. for liquid products, centrifuge at 200-500 RPM to gather the liquid at the bottom of the vial. try to avoid loss or contamination during handling.|
|1 mg||5 mg||10 mg||20 mg||25 mg|
|1 mM||2.6221 mL||13.1103 mL||26.2206 mL||52.4411 mL||65.5514 mL|
|5 mM||0.5244 mL||2.6221 mL||5.2441 mL||10.4882 mL||13.1103 mL|
|10 mM||0.2622 mL||1.311 mL||2.6221 mL||5.2441 mL||6.5551 mL|
|50 mM||0.0524 mL||0.2622 mL||0.5244 mL||1.0488 mL||1.311 mL|
|100 mM||0.0262 mL||0.1311 mL||0.2622 mL||0.5244 mL||0.6555 mL|
Eur J Med Chem. 2010 Sep;45(9):4288-92.
|Synthesis and anticancer activity of chromone-based analogs of lavendustin A.[Pubmed: 20630626]|
|Lavendustin A and hormothamnione were reported to exhibit cytotoxic effects on tumor cell lines. In the present studies, a series of chromone-based Lavendustin Analogs were synthesized as a simplified hybrid of hormothamnione and Lavendustin A by the reductive-amination of formyl-chromone 5 with various amines followed by aminoalkylation.|
J Biol Chem. 1991 Nov 5;266(31):21105-12.
|Kinetic analysis of the inhibition of the epidermal growth factor receptor tyrosine kinase by Lavendustin-A and its analogue.[Pubmed: 1939153 ]|
|Lavendustin A was reported to be a potent tyrosine kinase inhibitor of the epidermal growth factor (EGF) receptor (Onoda, T., Iinuma, H., Sasaki, Y., Hamada, M., Isshibi, K., Naganawa, H., Takeuchi, T., Tatsuta, K., and Umezawa, K. (1989) J. Nat. Prod. 52, 1252-1257). Its inhibition kinetics was studied in detail using the baculovirus-expressed recombinant intracellular domain of the EGF receptor (EGFR-IC). Lavendustin A (RG 14355) is a slow and tight binding inhibitor of the receptor tyrosine kinase. The difference between the two values is due to the tight binding nature of the inhibitor to the enzyme in EI*. The kinetic analysis using a preincubation protocol to pre-equilibrate the enzyme with the inhibitor in the presence of one substrate showed that Lavendustin A is a hyperbolic mixed-type inhibitor with respect to both ATP and the peptide substrate, with a major effect on the binding affinities for both substrates. An analogue of Lavendustin A (RG 14467) showed similar inhibition kinetics to that of Lavendustin A.|
J Med Chem. 2003 Apr 24;46(9):1670-82.
|Synthesis, anticancer activity, and inhibition of tubulin polymerization by conformationally restricted analogues of lavendustin A.[Pubmed: 12699385]|
|Compounds in the Lavendustin A series have been shown to inhibit both protein-tyrosine kinases (PTKs) and tubulin polymerization. Since certain Lavendustin A derivatives can exist in conformations that resemble both the trans-stilbene structure of the PTK inhibitor piceatannol and the cis-stilbene structure of the tubulin polymerization inhibitor combretastatin A-4, the possibility exists that the ratio of the two types of activities of the lavendustins could be influenced through the synthesis of conformationally restricted analogues. Accordingly, the benzylaniline structure of a series of pharmacologically active Lavendustin A fragments was replaced by either their cis- or their trans-stilbene relatives, and effects on both inhibition of tubulin polymerization and cytotoxicity in cancer cell cultures were monitored. Two of the Lavendustin A derivatives displayed IC(50) values of 1.4 microM for inhibition of tubulin polymerization, which ranks them among the most potent of the known tubulin polymerization inhibitors.|
Pflugers Arch. 1999 Feb;437(3):317-23.
|Angiotensin II stimulation of Ca2+-channel current in vascular smooth muscle cells is inhibited by lavendustin-A and LY-294002.[Pubmed: 9914387]|
|In the presence of Lavendustin A (5 microM), a selective inhibitor of Tyr-PK, AngII failed to stimulate IBa (n=5). AngII stimulation of IBa was also prevented by (5 microM) LY-294002, an inhibitor of PI-3-K (n=5). In contrast, H-7 (30 microM), an inhibitor of PKC, did not prevent the effect of AngII on IBa (n=6). These results suggest that AngII may stimulate the Ca2+ channels of VSM cells through Tyr-PK and PI-3-K under conditions that probably exclude participation of PK-C.|
Jpn J Pharmacol. 1997 Jun;74(2):203-8.
|Modulation of tyrosine kinase activity has multiple actions on insulin release from the pancreatic beta-cell: studies with lavendustin A.[Pubmed: 9243329]|
|Lavendustin A at 0.1 nM-1 microM caused a concave-shaped inhibition of the insulin release stimulated by 7 mM glucose. The inhibitory effect of Lavendustin A was overcome by higher concentrations of glucose. Lavendustin B, the negative control analogue, had no effect on the release. Lavendustin A at a nanomolar range progressively inhibited insulin release by high K+ (50 mM)-depolarization, whereas the inhibitor did not change the insulin release by Ca2+ ionophore (A23187). On the contrary, Lavendustin A at 10 nM significantly increased insulin release when glucose-induced insulin release was enhanced by either 5 microM forskolin or 162 nM 12-O-tetradecanoylphorbol 13-acetate. Lavendustin A failed to influence the Ca(2+)-induced insulin release from HIT cells permeabilized with streptolysin-O. These findings suggest that tyrosine kinases may play versatile roles in the control of insulin release from the pancreatic beta-cell.|