China Online Exporter Pharmaceutical Intermediates - Glutathione reduced Cas: 70-18-8 98-101% Clear and colourless – XD BIOCHEM Manufacturer and Supplier

Online Exporter Pharmaceutical Intermediates - Glutathione reduced Cas: 70-18-8 98-101% Clear and colourless – XD BIOCHEM

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To consistently enhance the management method by virtue of the rule of "sincerely, fantastic religion and top quality are the base of business development", we extensively absorb the essence of associated goods internationally, and constantly acquire new merchandise to satisfy the needs of shoppers for 77-86-1, D-Glucuronic Acid, Nitrotetrazolium Blue Chloride, Our main objectives are to provide our customers worldwide with good quality, competitive price, satisfied delivery and excellent services.

Online Exporter Pharmaceutical Intermediates - Glutathione reduced Cas: 70-18-8 98-101% Clear and colourless – XD BIOCHEM Detail:

Catalog Number	XD90284
Product Name	Glutathione reduced
CAS	70-18-8
Molecular Formula	C10H17N3O6S
Molecular Weight	307.32
Storage Details	2 to 8 °C
Harmonized Tariff Code	29309098

Product Specification

Assay	98% – 101%
Appearance	White crystalline powder
Grade	EP 7.0
Impurity A	<0.5%
Impurity B	<0.5%
Heavy metals	<10ppm
Bacterial endotoxin	<0.10EU/mg
Impurity C	<1.5%
Impurity D	<1.0%
Loss on Drying	<0.5%
Solubility	Freely soluble in water, slightly soluble in ethanol and methylene chloride
Iron	<10ppm
Chlorides	<200ppm
Appearance of Solution	Clear and colourless
Specific optical rotation	-15.5 to -17.5
Total Impurities	<2.5%
Ammonium	<200ppm
Sulfated ash	<0.1%
Sulphates	<300ppm
Impurity E	<0.5%

Post-translational protein modifications, such as tyrosine phosphorylation, regulate protein-protein interactions (PPIs) critical for signal processing and cellular phenotypes. We extended an established yeast two-hybrid system employing human protein kinases for the analyses of phospho-tyrosine (pY)-dependent PPIs in a direct experimental, large-scale approach. We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins and validated a large fraction in co-immunoprecipitation experiments from mammalian cells. About one-sixth of the interactions are mediated by known linear sequence binding motifs while the majority of pY-PPIs are mediated by other linear epitopes or governed by alternative recognition modes. Network analysis revealed that pY-mediated recognition events are tied to a highly connected protein module dedicated to signaling and cell growth pathways related to cancer. Using binding assays, protein compleme ntation and phenotypic readouts to characterize the pY-dependent interactions of TSPAN2 (tetraspanin 2) and GRB2 or PIK3R3 (p55γ), we exemplarily provide evidence that the two pY-dependent PPIs dictate cellular cancer phenotypes.

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