PBK Human
Description
PBK is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Lymphokine-activated killer T-cell-originated protein kinase (PBK), also known as MAP kinase-interacting serine/threonine kinase 2 (MKNK2), plays a crucial role in cellular processes like cell growth, differentiation, and survival. Primarily found in the placenta and testis, PBK participates in activating lymphoid cells and testicular functions, particularly spermatogenesis. Its activity is closely linked to mitosis, where phosphorylation is essential for its catalytic function. Upon phosphorylation, PBK interacts with the tumor suppressor protein TP53, affecting its stability and potentially influencing the G2/M cell cycle checkpoint, especially during DNA damage responses. The protein's activity is restricted to the mitotic phase. Additionally, PBK interacts with the Dlg protein, a tumor suppressor, through its PDZ domain and PBK's T/SXV motif. Further expanding its role, PBK phosphorylates MAP kinase p38, suggesting its involvement in lymphoid cell activation.
LHQEKKLLHG DIKSSNVVIK GDFETIKICD VGVSLPLDEN MTVTDPEACY IGTEPWKPKE AVEENGVITD KADIFAFGLT LWEMMTLSIP HINLSNDDDD EDKTFDESDF DDEAYYAALG TRPPINMEEL DESYQKVIEL FSVCTNEDPK DRPSAAHIVE ALETDV.
Product Science Overview
PBK is a protein that plays a crucial role in various cellular processes. It is composed of several structural domains, including the PDZ domain, which is a common protein interaction module. PDZ domains typically recognize short amino acid motifs at the C-termini of target proteins . These interactions are essential for regulating multiple biological processes such as transport, ion channel signaling, and other signal transduction systems .
PBK is expressed predominantly in the testis, specifically in the outer cell layer of seminiferous tubules, as well as in the placenta . It is involved in the activation of lymphoid cells and supports testicular functions, playing a role in spermatogenesis .
PBK functions as a mitotic kinase that phosphorylates MAP kinase p38 and is active during mitosis . When phosphorylated, PBK interacts with the tumor suppressor protein p53 (TP53), leading to the destabilization of TP53 and attenuation of the G2/M checkpoint during doxorubicin-induced DNA damage . This interaction suggests that PBK may play a role in cell cycle regulation and response to DNA damage.
Recombinant human PBK is produced using baculovirus-insect cell expression systems . The recombinant protein is typically purified to a high degree of purity, making it suitable for research purposes. It is often used in studies to understand the kinase’s role in cellular processes and its potential as a therapeutic target.
