Product nameRecombinant Human PKC delta protein
See all PKC delta proteins and peptides
Protein lengthFull length protein
Amino Acid Sequence
Molecular weight78 kDa
Our Abpromise guarantee covers the use of ab27714 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesNot enzymatically active. The protein is suspended in SDS/mercaptoethanol sample buffer with a bromphenol blue dye marker.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Constituents: 0.02% Bromophenol blue, 5% Beta mercaptoethanol, 2% SDS
- Kinase PKC delta
FunctionThis is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin.
Sequence similaritiesBelongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Contains 1 AGC-kinase C-terminal domain.
Contains 1 C2 domain.
Contains 2 phorbol-ester/DAG-type zinc fingers.
Contains 1 protein kinase domain.
DomainThe C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner.
modificationsPhosphorylated on Thr-507, within the activation loop. Autophosphorylated and/or phosphorylated. Although the Thr-507 phosphorylation occurs it is not a prerequisite for enzymatic activity.
Cellular localizationCytoplasm. Membrane.
- Information by UniProt
ab27714 has not yet been referenced specifically in any publications.