Pyrintegrin

Integrin and tyrosine kinase activator; Activates Integrin, FGFR, IGFR and HER2

Pyrintegrin

Integrin and tyrosine kinase activator; Activates Integrin, FGFR, IGFR and HER2

From: 104 USD
Catalog #
(Select a product)
Integrin and tyrosine kinase activator; Activates Integrin, FGFR, IGFR and HER2
Add to Wish List

Overview

Pyrintegrin is a 2,4-disubstituted pyrimidine that  induces the activation of β1 integrin and multiple growth factor receptors, including FGFR1, IGFR1, EGFR1, and HER2 (Xu et al.).

MAINTENANCE AND SELF-RENEWAL
· Enhances integrin-dependent attachment and survival of human embryonic stem (ES) cells following trypsin-mediated single-cell dissociation (Xu et al.).
Cell Type
Pluripotent Stem Cells
Species
Human, Mouse, Non-Human Primate, Other, Rat
Application
Maintenance
Area of Interest
Stem Cell Biology
CAS Number
1228445-38-2
Chemical Formula
C₂₃H₂₅N₅O₃S
Purity
≥ 95%
Pathway
Integrin, Tyrosine Kinase
Target
FGFR, HER2, IGFR, Integrin

Protocols and Documentation

Find supporting information and directions for use in the Product Information Sheet or explore additional protocols below.

Document Type
Product Name
Catalog #
Lot #
Language
Product Name
Pyrintegrin
Catalog #
72842, 72844
Lot #
All
Language
English
Document Type
Safety Data Sheet
Product Name
Pyrintegrin
Catalog #
72842, 72844
Lot #
All
Language
English

Applications

This product is designed for use in the following research area(s) as part of the highlighted workflow stage(s). Explore these workflows to learn more about the other products we offer to support each research area.

Resources and Publications

Publications (1)

Revealing a core signaling regulatory mechanism for pluripotent stem cell survival and self-renewal by small molecules. Xu Y et al. Proceedings of the National Academy of Sciences of the United States of America 2010 MAY

Abstract

Using a high-throughput chemical screen, we identified two small molecules that enhance the survival of human embryonic stem cells (hESCs). By characterizing their mechanisms of action, we discovered an essential role of E-cadherin signaling for ESC survival. Specifically, we showed that the primary cause of hESC death following enzymatic dissociation comes from an irreparable disruption of E-cadherin signaling, which then leads to a fatal perturbation of integrin signaling. Furthermore, we found that stability of E-cadherin and the resulting survival of ESCs were controlled by specific growth factor signaling. Finally, we generated mESC-like hESCs by culturing them in mESC conditions. And these converted hESCs rely more on E-cadherin signaling and significantly less on integrin signaling. Our data suggest that differential usage of cell adhesion systems by ESCs to maintain self-renewal may explain their profound differences in terms of morphology, growth factor requirement, and sensitivity to enzymatic cell dissociation.