cam-1

ICAM-1-IN-1 is a potent and selective inhibitor of E-selectin (IC50 = 7 nM) and ICAM-1 (IC50 = 5 nM).

ICAM-1988 is a LFA-1 antagonist.

Anti-CD54 ICAM-1 Antibody (R6-5-D6) is a chimeric mouse IgG2a antibody that specifically targets human CD54 ICAM-1. The recommended isotype control for this antibody is Mouse IgG2a kappa, Isotype Control.

Anti-Mouse CD106 VCAM-1 Antibody (M K-2.7) is an IgG1, κ inhibitor antibody derived from rats, specifically targeting mouse CD106 VCAM-1.

GLP-26 disrupts the encapsidation of pre-genomic RNA, causes nucleocapsid disassembly and reduces cccDNA pools. GLP-26 is a HBV capsid assembly modulators (CAM), inhibits HBV DNA replication in Hep AD38 system (IC50=3 nM), and reduces cccDNA by >90% at 1

Calmodulin antagonist-1 (W-7) is a calmodulin (CaM) antagonist that effectively inhibits calmodulin-activated Ca 2+ -phosphodiesterase (PDE) with an IC 50 of 28 μM. This compound also competitively inhibits trypsin-treated Ca 2+ -PDE with respect to cyclic GMP, exhibiting an IC 50 of 375 μM and a K i value of 300 μM.

Beauverolide Ja, a cyclotetradepsipeptide and secondary metabolite of Isaria fumosorosea [1], functions as a potent inhibitor of calmodulin (CaM), exhibiting a dissociation constant (Kd) of 0.078 μM and an inhibition constant (Ki) of 0.39 μM for Ca2+-CaM.

Syntide 2 (TFA), a substrate peptide for Ca2+- and calmodulin (CaM)-dependent protein kinase II (CaMKII), selectively inhibits the gibberellin (GA) response without affecting constitutive and abscisic acid-regulated events [1].

CALP2 TFA, a potent calmodulin (CaM) antagonist with a dissociation constant (Kd) of 7.9 µM, exhibits high affinity for the CaM EF-hand Ca2+-binding site. This compound effectively inhibits CaM-dependent phosphodiesterase activity and elevates intracellular Ca2+ concentrations. Furthermore, it significantly hinders adhesion and degranulation, while also acting as a robust activator of alveolar macrophages [1] [2] [3] [4].

CALP1 TFA, a calmodulin (CaM) agonist with a dissociation constant (Kd) of 88 µM, selectively binds to the CaM EF-hand Ca2+-binding site, inhibiting calcium channel opening. This action blocks calcium influx and apoptosis with an IC50 of 44.78 µM, modulates glutamate receptor channel activity, and impedes a store-operated nonselective cation channel. Additionally, CALP1 TFA enhances CaM-dependent phosphodiesterase activity, denoting its multifaceted role in modulating cellular calcium dynamics [1] [2] [3] [4].

Neurogranin (48-76), mouse, is a peptide comprising residues 48-76 of Neurogranin, a post-synaptically exclusive calmodulin-binding protein that mediates NMDAR-driven synaptic plasticity by regulating the calcium-calmodulin (Ca2+-CaM) pathway [1].

Calmodulin-Dependent Protein Kinase Substrate Analog, a synthetic peptide substrate, is activated by Ca2+ and calmodulin (CaM). It serves as a substrate for protein kinases, leveraging a dependency on Ca2+ and CaM for its function [1].

Calmodulin Dependent Protein Kinase Substrate is a synthetic peptide that interacts specifically with calmodulin-dependent protein kinases (CaMK) and requires calcium ions (Ca 2+) and calmodulin (CaM) for activation. It is utilized in studies involving protein kinase activity [1].

15-Deoxy-Δ12,14-Prostaglandin A1, a deoxyanalog of prostaglandins, inhibits NF-κB signaling and induces apoptosis. It also prevents TNF-α-induced upregulation of inflammatory endothelial cell adhesion molecules (CAM) and reduces monocyte arrest [1].

Calmodulin Binding Peptide 1, a potent CaM-binding peptide with picomolar (pM) affinity, originates from smooth muscle myosin light-chain kinase (MLCK peptide). It effectively blocks inositol trisphosphate (IP3)-induced calcium (Ca2+) release [1].

Cell-permeable calmodulin (CaM) agonist that binds to the EF-hand/Ca2+-binding site; produces CaM-dependent activation of phosphodiesterase. Also binds to cytoplasmic sites on other Ca2+ channels, including NMDA and HIV-1 gp120-activated channels, inhibit

MLCK Peptide, a high-affinity (pM), fully reversible CaM-binding peptide, is derived from smooth muscle myosin light-chain kinase [1].

CaMKI (299-320) is a peptide representing residues 299-320 of Calcium calmodulin-dependent protein kinase I (CaMKI). This segment, functioning as a protein kinase, exhibits a strong interaction with Ca 2+ -CAM (K d ≤1 nM), enabling it to phosphorylate specific substrate proteins and regulate their activity. It encompasses both the CAM-binding domain and the self-inhibition domain. CaMKI (299-320) is applicable for researching cellular physiological processes such as proliferation, differentiation, and apoptosis .