Life Science

A competitive inhibitor of nucleotide binding by Ras-related GTPases binds Rab7 (Ki = 13 nM), preventing BODIPY-linked GTP and GDP binding with EC₅₀ values of 11.2 and 21 nM, respectively.

A competitive inhibitor of nucleotide binding by Ras-related GTPases binds Rab7 (Ki = 13 nM), preventing BODIPY-linked GTP and GDP binding with EC₅₀ values of 11.2 and 21 nM, respectively.

A competitive inhibitor of nucleotide binding by Ras-related GTPases binds Rab7 (Ki = 13 nM), preventing BODIPY-linked GTP and GDP binding with EC₅₀ values of 11.2 and 21 nM, respectively.

A competitive inhibitor of nucleotide binding by Ras-related GTPases binds Rab7 (Ki = 13 nM), preventing BODIPY-linked GTP and GDP binding with EC₅₀ values of 11.2 and 21 nM, respectively.

An inhibitor of all three PKD isoforms (IC₅₀s = 3.2, 0.

An inhibitor of all three PKD isoforms (IC₅₀s = 3.2, 0.

An inhibitor of all three PKD isoforms (IC₅₀s = 3.2, 0.

A reversible, competitive antagonist of GPR35, blocking activation by the synthetic agonist pamoic acid with a Ki of 12.8 nM less potently blocks activation of GPR35 by zaprinast (IC50 = 160 nM) shows ~57-fold selectivity for GPR35 over the

A reversible, competitive antagonist of GPR35, blocking activation by the synthetic agonist pamoic acid with a Ki of 12.8 nM less potently blocks activation of GPR35 by zaprinast (IC50 = 160 nM) shows ~57-fold selectivity for GPR35 over the

A reversible, competitive antagonist of GPR35, blocking activation by the synthetic agonist pamoic acid with a Ki of 12.8 nM less potently blocks activation of GPR35 by zaprinast (IC50 = 160 nM) shows ~57-fold selectivity for GPR35 over the

A reversible, competitive antagonist of GPR35, blocking activation by the synthetic agonist pamoic acid with a Ki of 12.8 nM less potently blocks activation of GPR35 by zaprinast (IC50 = 160 nM) shows ~57-fold selectivity for GPR35 over the

A selective inhibitor of PKC-induced NF-&kappaB pathway activation (IC₅₀ = 0.07 &muM) inhibits IL-8 production in HEK293 cells (IC₅₀ &le 0.