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Tyrphostin AG30 Sale

(Synonyms: 酪氨酸磷酸化抑制剂AG30,AG30) 目录号 : GC38125

Tyrphostin AG30 (AG30), a potent and selective EGFR tyrosine kinase inhibitor, selectively inhibits self renewal induction by c-ErbB, and is able to inhibit activation of STAT5 by c-ErbB in primary erythroblasts.

Tyrphostin AG30 Chemical Structure

Cas No.:122520-79-0

规格 价格 库存 购买数量
10mM (in 1mL DMSO)
¥508.00
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2mg
¥450.00
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5mg
¥720.00
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10mg
¥900.00
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25mg
¥1,980.00
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50mg
¥3,510.00
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100mg
¥5,850.00
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200mg 待询 待询
500mg 待询 待询

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产品描述

Tyrphostin AG30 (AG30), a potent and selective EGFR tyrosine kinase inhibitor, selectively inhibits self renewal induction by c-ErbB, and is able to inhibit activation of STAT5 by c-ErbB in primary erythroblasts.

[1] Wessely O, et al. Cell Growth Differ. 1997 May;8(5):481-93.

Chemical Properties

Cas No. 122520-79-0 SDF
别名 酪氨酸磷酸化抑制剂AG30,AG30
Canonical SMILES O=C(/C(C#N)=C/C1=CC=C(C(O)=C1)O)O
分子式 C10H7NO4 分子量 205.17
溶解度 DMSO: 125 mg/mL (609.25 mM) 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 4.874 mL 24.37 mL 48.7401 mL
5 mM 0.9748 mL 4.874 mL 9.748 mL
10 mM 0.4874 mL 2.437 mL 4.874 mL
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Research Update

Distinct roles of the receptor tyrosine kinases c-ErbB and c-Kit in regulating the balance between erythroid cell proliferation and differentiation

Cell Growth Differ 1997 May;8(5):481-93.PMID:9149900doi

In the bone marrow, multipotent and committed hematopoietic progenitors have to closely regulate their balance between sustained proliferation without differentiation (self renewal) and entering a terminal differentiation pathway. A useful model to analyze this regulation at the molecular level is committed avian erythroid progenitors. These are induced to undergo long-term self renewal by the ligand-activated receptor tyrosine kinase (RTK) c-ErbB, in cooperation with steroid hormone receptors. This self-renewal induction by c-ErbB even occurs in the presence of differentiation factors (erythropoietin and insulin). Under the same conditions, the RTK c-Kit is unable to sustain erythroid progenitor self renewal, stimulating cell proliferation without arresting terminal differentiation. Two mechanisms are involved in these differential activities of c-Kit and c-ErbB. The first one, differential regulation of receptor expression, proved to be of minor importance, because c-Kit was unable to induce self renewal, even if exogenously expressed from a retrovirus at high levels. Rather our results support the second mechanism, i.e., that receptor-specific signal transduction is responsible for the differential biological activity of c-Kit and c-ErbB: (a) specific tyrosine kinase inhibitors (tryphostins) were found which selectively inhibited the biological function of either c-Kit or c-ErbB in erythroblasts but did not affect ligand-induced autophosphorylation of either RTK; and (b) c-ErbB selectively induced SHC phosphorylation and STAT5 activation. The Ras pathway was similarly activated by c-Kit and c-ErbB. The c-ErbB-specific Tyrphostin AG30 specifically blocked STAT5 activation, implicating this signal transducer in c-ErbB-induced self renewal.