|Detection of Human/Mouse PKC iota / lambda by Western Blot. Western blot shows lysates of A431 human epithelial carcinoma cell line, DU145 human prostate carcinoma cell line, and NIH‑3T3 mouse embryonic fibroblast cell line. PVDF membrane was probed with 1 µg/mL of Human/Mouse PKC iota / lambda Monoclonal Antibody (Catalog # MAB4465) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for PKC iota / lambda at approximately 78 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 cofactor requirements: conventional PKC isoforms ( alpha, beta Ι, beta II, 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 iota is highly expressed in brain and lung but is also expressed at lower levels in many tissues including pancreatic islets. It is the catalytic component of the Par3-Par6-atypical PKC complex, a key regulator of the formation and maintenance of epithelial cell polarity, adherens junctions, and tight junctions. PKC iota has also been shown to be critical for Ras-mediated transformation, invasion, and anchorage‑independent growth of intestinal epithelial cells. The rodent homolog is termed PKC lambda and is 95% homologous to PKC iota.