Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Purity: > 80% Densitometry
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE
Product nameRecombinant X. laevis PKC alpha protein
See all PKC alpha proteins and peptides
Purity> 80 % Densitometry.
Expression systemBaculovirus infected Sf9 cells
Protein lengthFull length protein
DescriptionRecombinant X. laevis PKC alpha protein
Our Abpromise guarantee covers the use of ab60839 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ab204856 (CREB peptide) can be utilized as a substrate for assessing kinase activity
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.0038% EGTA, 0.00174% PMSF, 0.00385% DTT, 0.79% Tris HCl, 0.00292% EDTA, 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Aging associated gene 6
FunctionThis is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4.
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.
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.
Cellular localizationCytoplasm. Cell membrane. Nucleus.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab60839 has not yet been referenced specifically in any publications.