314045-39-1 | Bptes

Packsize	Purity	Availability	Price	Discounted Price
1mg	95%	in stock	$28.00	$19.00
5mg	95%	in stock	$56.00	$39.00
10mg	95%	in stock	$58.00	$40.00
25mg	95%	in stock	$100.00	$70.00
100mg	95%	in stock	$210.00	$147.00
250mg	95%	in stock	$438.00	$306.00
1g	95%	in stock	$1,345.00	$941.00

Description

• Catalog Number: AB71360
• Chemical Name: Bptes
• CAS Number: 314045-39-1
• Molecular Formula: C24H24N6O2S3
• Molecular Weight: 524.6814
• MDL Number: MFCD01079848
• SMILES: O=C(Cc1ccccc1)Nc1nnc(s1)CCSCCc1nnc(s1)NC(=O)Cc1ccccc1

Computed Properties

• Complexity: 609
• Covalently-Bonded Unit Count: 1
• Heavy Atom Count: 35
• Hydrogen Bond Acceptor Count: 9
• Hydrogen Bond Donor Count: 2
• Rotatable Bond Count: 12
• XLogP3: 4

Upstream Synthesis Route

BPTES (Bis-2-(5-phenylacetamido-1,3,4-thiadiazol-2-yl)ethyl sulfide) is a potent and selective inhibitor of the enzyme glutaminase. Glutaminase is an enzyme involved in the conversion of glutamine to glutamate, an important process in various cellular functions including energy production and biosynthesis.In chemical synthesis, BPTES is utilized as a tool compound to specifically target and inhibit glutaminase activity. By blocking the function of glutaminase, BPTES can modulate the metabolic pathways that rely on glutamine metabolism. This can be particularly useful in studying the role of glutamine in cancer metabolism, as many cancer cells exhibit an increased dependence on glutamine for their growth and proliferation.Furthermore, BPTES can be employed in the development of novel therapeutic strategies targeting glutamine metabolism in cancer cells. By understanding the mechanisms by which BPTES interferes with glutaminase activity, researchers can potentially design new drugs that selectively target cancer cells while sparing normal cells.Overall, the application of BPTES in chemical synthesis provides a valuable tool for studying glutamine metabolism and potentially developing new treatments for cancer and other diseases characterized by dysregulated metabolic processes.

Literature

• Full-length human glutaminase in complex with an allosteric inhibitor.

  Biochemistry 20111220