Items 121 to 123 of 123 total
Display:
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING | 
|---|---|---|---|---|---|---|
Adaphostin | 241127-58-2 | sc-291833 sc-291833A  | 10 mg 50 mg  | $129.00 $560.00  | ||
Adaphostin acts as a tyrosine kinase inhibitor, characterized by its ability to disrupt ATP binding through unique steric hindrance. This compound selectively targets specific kinase domains, leading to altered phosphorylation states of key substrates. Its structural conformation allows for precise interactions with the active site, influencing downstream signaling cascades. Additionally, Adaphostin's electronic characteristics may enhance its binding affinity, contributing to its distinct kinetic profile in kinase modulation.  | ||||||
Imatinib-d8 | 1092942-82-9 | sc-488072 sc-488072A  | 1 mg 10 mg  | $556.00 $4085.00  | ||
Imatinib-d8 functions as a selective tyrosine kinase inhibitor, exhibiting unique isotopic labeling that enhances its tracking in biochemical assays. Its deuterated structure influences reaction kinetics, potentially altering metabolic stability and interaction dynamics. The compound's specific binding affinity to the ATP site is modulated by its conformational flexibility, allowing for tailored interactions with various kinase isoforms. This specificity can lead to distinct downstream signaling alterations, providing insights into kinase regulation.  | ||||||
3-Amino-5-nitrobenzoic acid | 618-84-8 | sc-276008 sc-276008A  | 1 g 5 g  | $64.00 $180.00  | ||
3-Amino-5-nitrobenzoic acid exhibits unique properties as a tyrosine kinase modulator, where its nitro group significantly alters the electronic environment, enhancing binding affinity to target proteins. The compound's structural features facilitate specific hydrogen bonding interactions, which can stabilize enzyme-substrate complexes. This stabilization may influence the phosphorylation process, affecting downstream signaling pathways and cellular responses, thereby showcasing its role in biochemical interactions.  | ||||||