Recombinant human Protein Kinase C (PKC) alpha, 10 µg

Background: Protein kinase C (PKC) is a family of serine-threonine kinases, which are classified into three major groups: classical (α, β and γ), novel (δ, ε, η, and θ) and atypical (μ, ξ and ι). Protein kinase C alpha (PKC alpha) is an ubiquitously expressed PKC isoform which is activated in response to many different kinds of stimuli causing translocation from the cytosol to specialized cellular compartments. Therefore, PKC alpha has been implicated in a variety of cellular functions including proliferation, apoptosis, differentiation, motility, and inflammation which are modulated by dynamic interactions with cell-type specific factors, substrates, modulators and PKC anchoring proteins.

Recombinant human PKC alpha, recombinantly expressed in Sf9 cells, N-terminally fused to GST-HIS6-Thrombin cleavage site

Protein:  Human PKC-alpha, full length, amino acids M1-V672, N-terminal GST-HIS6 fusion protein with a Thrombin cleavage site
Theoretical MW:           109.972 kDa (fusion proteins)
Expression system:    Baculovirus infected Sf9 cells
Purification:                One-step affinity purification using GSH-agarose
Storage buffer:            50 mM Tris-HCl, pH 8.0; 100 mM NaCl, 5 mM DTT, 15 mM reduced glutathione, 20% glycerol
Storage temperature: - 80°C (avoid repeated freeze-thaw cycles !)
Protein concentration: 0.17 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSFC membrane
Specific activity:         526.000 pmol/mg min (1 Unit is defined as 1 picomole phosphate transferred to PKC substrate (Histone H1) per min)

Entrez Gene ID: 5578   
UniProtKB: P17252

Ordering information: shipped on dry ice

Product specific literature references

Sozeri O, Vollmer K, Liyanage M, Frith D, Kour G, Mark GE 3rd, Stabel S (1992) "Activation of the c-Raf protein kinase by protein kinase C phosphorylation" Oncogene 7(11):2259-62

Gruber JR, Ohno S, Niles RM (1992) "Increased expression of protein kinase C alpha plays a key role in retinoic acid-induced melanoma differentiation" J Biol Chem. 267(19):13356-60

Kolch W, Heidecker G, Kochs G, Hummel R, Vahidi H, Mischak H, Finkenzeller G, Marme D, Rapp UR (1993) "Protein kinase C alpha activates RAF-1 by direct phosphorylation" Nature 364(6434):249-52

Mischak H, Pierce JH, Mushinski JF et al. (1993) "Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-alpha and -delta and not by protein kinase C-beta II, -epsilon, -zeta, and -eta" J Biol Chem. 268(27):20110-5

Carroll MP, May WS (1994) "Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells" J Biol Chem 269(2):1249-56

Newton AC (1995) "Protein kinase C: structure, function, and regulation" J Biol Chem. 270(48):28495-8

Bornancin F, Parker PJ (1996) "Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Calpha" Curr Biol. 6(9):1114-23

Uberall F, Giselbrecht S, Baier G et al. (1997) "Conventional PKC-alpha, novel PKC-epsilon and PKC-theta, but not atypical PKC-lambda are MARCKS kinases in intact NIH 3T3 fibroblasts" J Biol Chem. 272(7):4072-8

Newton AC (1997) "Regulation of protein kinase C" Curr Opin Cell Biol. 9(2):161-7

Ng T, Squire A, Parker PJ et al. (1999) "Imaging protein kinase Calpha activation in cells" Science 283(5410):2085-9

Braz JC, Bueno OF, De Windt LJ, Molkentin JD (2002) "PKC alpha regulates the hypertrophic growth of cardiomyocytes through extracellular signal-regulated kinase1/2 (ERK1/2)" J Cell Biol. 156(5):905-19

Lahn M, Kohler G, Bumol TF et al. (2004) "Protein kinase C alpha expression in breast and ovarian cancer" Oncology 67(1):1-10