Lane 1: Hela cell lysate
Lane 2: NIH/3T3 cell lysate
Recombinant Rabbit monoclonal primary
PKC delta Recombinant Rabbit Monoclonal Antibody [JJ093-02] (ET1701-85)
Recombinant protein within mouse pkc delta aa 530-674.
Hela cell lysate, NIH/3T3 cell lysate, A549, MCF-7, HepG2, RH-35, human tonsil tissue, human liver tissue, human spleen tissue, human breast carcinoma tissue, mouse testis tissue, mouse liver tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
CVID9 antibody; D14Ertd420e antibody; Kinase PKC delta antibody; KPCD antibody; KPCD_HUMAN antibody; MAY 1 antibody; MAY1 antibody; MGC49908 antibody; nPKC delta antibody; nPKC-delta antibody; PCKd antibody; PKC d antibody; PKC delta antibody; PKCD antibody; PKCdelta antibody; PRKC D antibody; PRKC delta antibody; Prkcd antibody; Protein Kinase C delta antibody; Protein kinase C delta type antibody; Protein kinase C delta VIII antibody; Protein Kinase Cdelta antibody; Tyrosine protein kinase PRKCD antibody
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Autophosphorylated and/or phosphorylated at Thr-507, within the activation loop; phosphorylation at Thr-507 is not a prerequisite for enzymatic activity. Autophosphorylated at Ser-299, Ser-302 and Ser-304. Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-155; phosphorylation is required for its translocation to the endoplasmic reticulum and cleavage by caspase-3. Phosphorylated at Tyr-313, Tyr-334 and Tyr-567; phosphorylation of Tyr-313 and Tyr-567 following thrombin stimulation potentiates its kinase activity. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2.; Proteolytically cleaved into a catalytic subunit and a regulatory subunit by caspase-3 during apoptosis which results in kinase activation.
Cytoplasm, Nucleus, Cell membrane.
Members of the protein kinase C (PKC) family play a key regulatory role in a variety of cellular functions, including cell growth and differentiation, gene expression, hormone secretion and membrane function. PKCs were originally identified as serine/threonine protein kinases whose activity was dependent on calcium and phospholipids. Diacylglycerols (DAG) and tumor promoting phorbol esters bind to and activate PKC. PKCs can be subdivided into at least two major classes, including conventional (c) PKC isoforms (α, βI, βII and γ) and novel (n) PKC isoforms (δ, ε, ζ, η, θ, λ/ι, μ and ν). Patterns of expression for each PKC isoform differ among tissues and PKC family members exhibit clear differences in their cofactor dependencies. For instance, the kinase activities of PKC δ and ε are independent of Ca2+. On the other hand, most of the other PKC members possess phorbol ester-binding activities and kinase activities.