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CdA/CdQ

658390

AG 9 - CAS 2826-26-8 - Calbiochem

Name: AG 9 - CAS 2826-26-8 - Calbiochem
Brand: MM

Sinonimo/i:

[(4-Methoxybenzylidene)malononitrile, α-Cyano-(4-methoxy)cinnamonitrile], Tyrphostin A1

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About This Item

Codice UNSPSC:

12352200

Saggio

≥98% (TLC)

Livello qualitativo

100

Forma fisica

solid

Colore

yellow

Solubilità

ethanol: 10 mg/mL
DMSO: soluble
acetic acid: soluble

Descrizione generale

An inactive compound that can be used as a negative control for inhibition of EGFR (IC₅₀ >1250 μM for EGFR kinase). Has been shown to inhibit IL-2 stimulated Tyk-2 phosphorylation in ConA-activated T cells.

Azioni biochim/fisiol

negative control for inhibition of EGFR

Target IC<SUB>50</SUB>:>1250 μM for EGFR kinase

Ricostituzione

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.

Codice della classe di stoccaggio

10-13 - German Storage Class 10 to 13

Certificati d'analisi (COA)

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Effects of tyrphostins and genistein on the circulatory failure and organ dysfunction caused by endotoxin in the rat: a possible role for protein tyrosine kinase.

H Ruetten et al.

British journal of pharmacology, 122(1), 59-70 (1997-09-23)

1 Here we compared the effects of various inhibitors of the activity of protein tyrosine kinase on (i) the expression of the activity of the inducible isoform of nitric oxide (NO) synthase (iNOS) caused by endotoxin (lipopolysaccharide, LPS) in cultured

Tyrphostin B42 inhibits IL-12-induced tyrosine phosphorylation and activation of Janus kinase-2 and prevents experimental allergic encephalomyelitis.

J J Bright et al.

Journal of immunology (Baltimore, Md. : 1950), 162(10), 6255-6262 (1999-05-07)

IL-12 is a macrophage-derived cytokine that induces proliferation, cytokine production, and cytotoxic activity of T and NK cells. Signaling through its receptor, IL-12 induces these cellular responses by tyrosine phosphorylation and activation of Janus kinase-2 (Jak-2), Tyk-2, Stat3, and Stat4.

Tyrphostins I: synthesis and biological activity of protein tyrosine kinase inhibitors.

A Gazit et al.

Journal of medicinal chemistry, 32(10), 2344-2352 (1989-10-01)

A novel class of low molecular weight protein tyrosine kinase inhibitors is described. These compounds constitute a systematic series of molecules with a progressive increase in affinity toward the substrate site of the EGF receptor kinase domain. These competitive inhibitors

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