Product Name: PBK (3-22)
Product Number: PE-01BEI70
Size: 200 µg      Price:14.00
1 mg      $US29.00
5 mg      78.00
Peptide Name: PBK (3-22)

Product Use: Services as a blocking peptide for use with the PBK-NT rabbit polyclonal antibody (Cat. No.: AB-NK284-1) that is also available from Kinexus. The peptide sequence is located in the N-terminus.

Peptide Production Method: Solid-phase peptide synthesis

Peptide Origin: Homo sapiens

Peptide Sequence: GISNFKTPSKLSEKKKSVLC

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: Amide

Peptide Molecular Mass Calculated: 2193.6 Da

Peptide Purity Percent after Synthesis and Purification: >50

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Related Product 1: PBK pan-specific antibody (Cat. No.: AB-NK284-1)

Scientific Background: PBK (also known as TOPK) is a protein-serine/threonine kinase that is a member of the Other group of protein kinases in the TOPK family. This kinase shows high variability in human tissue distribution with the highest levels detected in lymph nodes, pituitary, spleen, testes and tonsils. Expression of PKB is particularly detected in male germ line progenitor cells, activated T-cells, and a variety of lymphomas and leukemias. T9 phosphorylation of PBK by CDK1 increases its phosphotransferase activity and induces interaction with CCNB1, CDK1, and tubulin-alpha1. PASK phosphorylates p38 MAPK (but not JNK or ERK1/2) and is activated in a cell-cycle-dependent manner in neuronal progenitor cells in vitro. PBK is active in mitosis and inhibition of the PBK/p38 pathway disrupts neural progentior proliferation and self renewal. In addition, PBK is hypothesized to function in the activation of lymphoid cells. When activated, PBK forms a complex with p53, which destablizes the p53 protein and leads to the attenuation of the G2/M checkpoint for DNA damage. PKB activation requires phosphorylation by both the M-phase CDK1/CyclinB kinase complex and another unknown kinase, possibly Raf1 or RafA. PKB may play an important role in linking extracellular signals to an intracellular state, possibly allowing extracellular influence on the cell-cycle-related processes of proliferation or differentiation. PBK may be an oncoprotein (OP). Gain-of-function mutations in PBK are linked to cancer, specifically plexiform neuroblastoma, as an overactive PBK protein impairs the G2/M checkpoint and prevents cell cycle arrest in the presence of DNA damage. Despite being absent from most normal somatic tissues, PBK has been shown to be significantly upregulated in several cancer types, indicating that gain-of-function mutations may be causing aberrant PBK expression leading to the augmentation of tumour growth in several forms of human cancer.