|Detection of Human PKC beta 2 by Western Blot. Western blot shows lysates of human brain tissue, mouse brain tissue, and K562 human chronic myelogenous leukemia cell line. PVDF membrane was probed with 1 µg/mL of Human/Mouse PKC beta 2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4378) followed by HRP-conjugated Anti‑Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for PKC beta 2 at approximately 90 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Members of the Protein Kinase C (PKC) family are serine/threonine protein kinases that play a key regulatory role in a number of cellular functions including cell growth and differentiation, hormone secretion, and gene expression. Multiple genes and alternative splicing result in three subfamilies, which differ in their co‑factor requirements: conventional PKC isoforms ( alpha, beta 1, beta 2, and gamma ) which require calcium and phosphatidylserine (PS), diacylglycerol (DAG) or phorbol esters for activation; novel isoforms (δ, epsilon, eta, and theta ), which are calcium-independent but are still regulated by PS, DAG, or phorbol esters; and atypical isoforms ( iota / lambda, and zeta ), which are calcium-independent and do not require PS, DAG, or phorbol esters for activation. PKC beta 2 regulation of c-myc expression has been shown to suppress insulin gene transcription in pancreatic beta -cells implicating PKC beta 2 for some of the beta -cell glucose toxicity found in diabetes.