Phospho-CD28 (Tyr191) (E5B9Z) Rabbit mAb recognizes endogenous levels of CD28 protein only when phosphorylated at Tyr191. This antibody shows cross-reactivity with phosphorylated EGFR, ERBB2, and CSF1R, and detects a 70-80 kDa band of unknown origin in some treated cell lines.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr191 of human CD28 protein.

CD28 is a transmembrane glycoprotein expressed by T cells as well as some other hematopoietic cells (1, 2). T cell activation requires T cell receptor (TCR) recognition of antigen presented in the context of MHC molecules. CD28 acts as a T cell costimulatory receptor, and interaction of CD28 with its ligands CD80 or CD86 provides the second signal required for naïve T cell activation (3-5). Activation of naïve T cells in the absence of CD28 stimulation can result in a state of T cell anergy, or unresponsiveness (3). CD28 signals through cytoplasmic phospho-tyrosine motifs that bind several SH2 or SH3 domain-containing proteins involved in T cell activation (2). Recently, CD28 was demonstrated to be a preferred target of PD-1-mediated dephosphorylation. Consistently, CD28 expression was required for T cell proliferation following PD-1 blockade and CD28 stimulation was required for effective anti-PD-1 cancer immunotherapy in mice (6, 7). Several CD28 isoforms are produced by alternative splicing (8).