Recombinant human serine/threonine protein kinase PIM1 dephosphorylated, 20 µg

Background: PIM-1 is a serine/ threonine kinase belonging to the group of calcium/calmodulin-regulated kinases (CAMK). As an artifact of bacterial expression the human Pim-1 N-terminus is multiple phosphorylated. Crystal structures of non-phosphorylated Pim-1 kinase demonstrate that the catalytic region adopts a constitutive active confirmation and phosphorylation does not influence its activity. The kinase is involved in the regulation of cell cycle progression and apoptosis by phosphorylating e.g. Cdc25A, Cdc25C, C-TAK1, Bad and FOXO3a.  Human PIM-1 has multiple roles in tumorigenesis. It promotes early transformation, cell proliferation and cell survival. In addition it may have a role in angiogenesis and vasculogenesis as a downstream effector of the VEGF-A/Flk1 pathway. PIM-1 expression is correlated with tumor aggressiveness and is a marker for poor prognosis. PIM-1 expression can be predictive of tumour outcome following chemotherapy and surgery and has been correlated with the enhanced metastatic potential of the tumor.

Protein: Purified and dephosphorylated recombinant human PIM-1 expressed in E.coli. 

Protein concentration: 0.67 mg/ml (Bradford method using BSA as standard protein)
Purification:  Expressed in E.coli, purification using Ni-NTA agarose, ion exchange chromatography and gel filtration
Purity: > 95% by SDS PAGE
Specific activity : 3,800,000 Units*/ mg (1Unit is defined as 1 picomole phosphate transferred to synthetic peptide (KKRNRTLTV) per min at 30 °C)
Theoretical MW (PIM-1): 37.4 kDa (fusion protein)

Entrez Gene ID: 5292
UniProtKB:  P11309

Ordering information: shipped on dry ice

Product specific literature:

Shah N, Pang B, Yeoh KG, Thorn S, Chen CS, Lilly MB, Salto-Tellez M. (2008) "Potential roles for the PIM1 kinase in human cancer – A molecular and therapeutic appraisal" Eur J Cancer. 44(15):2144-51.

Qian KC, Wang L, Hickey ER, Studts J, Barringer K, Peng C, Kronkaitis A, Li J, White A, Mische S, Farmer B.(2005) “Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase.” J Biol Chem. 18;280(7):6130-7.

Swords R, Kelly K, Carew J, Nawrocki S, Mahalingam D, Sarantopoulos J, Bearss D, Giles F. (2011) “The Pim Kinases: New Targets for Drug Development.” Curr Drug Targets.

Bachmann M, Möröy T. (2005) "The serine/threonine kinase Pim-1." Int J Biochem Cell Biol. 37(4):726-30.

Kim J, Roh M, Abdulkadir SA. (2010) "Pim1 promotes human prostate cancer cell tumorigenicity and c-MYC transcriptional activity." BMC Cancer. 1;10:248.

Bullock AN, Debreczeni J, Amos AL, Knapp S, Turk BE. (2005)„Structure and substrate specificity of the Pim-1 kinase.” J Biol Chem. 280(50):41675-82.