PLK2 Antibody [M21F17] Datasheet

Biological Description

Specificity	PLK2 Antibody [M21F17] detects endogenous levels of total PLK2 protein.
Background	Polo-like kinase 2 (PLK2), also known as serum- and glucocorticoid-inducible kinase SNK, is a serine/threonine kinase of the polo-like kinase family that links cell-cycle control and neuronal signaling by integrating p53-dependent checkpoint regulation, centriole duplication, and small GTPase-mediated synaptic plasticity. The protein shares the canonical organization of PLKs with an N-terminal catalytic kinase domain and C-terminal polo-box domains that recognize prephosphorylated motifs and localize PLK2 to defined subcellular structures, which permits context-specific phosphorylation of substrates involved in centrosome duplication, spindle checkpoint function, and Ras/Rap signaling complexes. During the cell cycle, PLK2 acts at the G1/S boundary and early mitotic events, where its kinase activity contributes to procentriole formation and accurate centriole replication, and its p53-inducible transcriptional control links centrosome duplication to DNA-damage and replication checkpoints, placing PLK2 in pathways that safeguard genomic integrity under proliferative and stress conditions. In neurons, PLK2 functions as a homeostatic suppressor of overexcitation and a key organizer of structural plasticity by coordinating the activity balance of Ras and Rap small GTPases at excitatory synapses; the kinase phosphorylates the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 to promote their degradation, while also phosphorylating the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1 to enhance their function, which shifts signaling away from Ras and toward Rap and thereby drives activity-dependent spine remodeling and adjusts synaptic strength. This bidirectional control of GEFs and GAP-like regulators situates PLK2 as an upstream timing and gain regulator for Ras–ERK and Rap-dependent cascades that influence AMPA receptor trafficking, dendritic spine density, and memory-related circuit refinement. PLK2 also modifies α-synuclein at regulatory sites that affect its turnover and aggregation, linking the kinase to proteostatic mechanisms that limit toxic protein accumulation and suggesting a functional interface between PLK2 activity, autophagic α-synuclein clearance, and neuronal resilience in synucleinopathies. PLK2 expression shows features of a stress-responsive kinase with context-dependent tumor suppressor properties; its p53-driven induction and roles in centriole duplication and checkpoint control connect PLK2 loss or silencing to centrosome abnormalities, cell-cycle deregulation, and chemoresistance, while retained or elevated PLK2 activity correlates with improved treatment response in specific cancer settings.

Specificity

PLK2 Antibody [M21F17] detects endogenous levels of total PLK2 protein.

Background

Polo-like kinase 2 (PLK2), also known as serum- and glucocorticoid-inducible kinase SNK, is a serine/threonine kinase of the polo-like kinase family that links cell-cycle control and neuronal signaling by integrating p53-dependent checkpoint regulation, centriole duplication, and small GTPase-mediated synaptic plasticity. The protein shares the canonical organization of PLKs with an N-terminal catalytic kinase domain and C-terminal polo-box domains that recognize prephosphorylated motifs and localize PLK2 to defined subcellular structures, which permits context-specific phosphorylation of substrates involved in centrosome duplication, spindle checkpoint function, and Ras/Rap signaling complexes. During the cell cycle, PLK2 acts at the G1/S boundary and early mitotic events, where its kinase activity contributes to procentriole formation and accurate centriole replication, and its p53-inducible transcriptional control links centrosome duplication to DNA-damage and replication checkpoints, placing PLK2 in pathways that safeguard genomic integrity under proliferative and stress conditions. In neurons, PLK2 functions as a homeostatic suppressor of overexcitation and a key organizer of structural plasticity by coordinating the activity balance of Ras and Rap small GTPases at excitatory synapses; the kinase phosphorylates the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 to promote their degradation, while also phosphorylating the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1 to enhance their function, which shifts signaling away from Ras and toward Rap and thereby drives activity-dependent spine remodeling and adjusts synaptic strength. This bidirectional control of GEFs and GAP-like regulators situates PLK2 as an upstream timing and gain regulator for Ras–ERK and Rap-dependent cascades that influence AMPA receptor trafficking, dendritic spine density, and memory-related circuit refinement. PLK2 also modifies α-synuclein at regulatory sites that affect its turnover and aggregation, linking the kinase to proteostatic mechanisms that limit toxic protein accumulation and suggesting a functional interface between PLK2 activity, autophagic α-synuclein clearance, and neuronal resilience in synucleinopathies. PLK2 expression shows features of a stress-responsive kinase with context-dependent tumor suppressor properties; its p53-driven induction and roles in centriole duplication and checkpoint control connect PLK2 loss or silencing to centrosome abnormalities, cell-cycle deregulation, and chemoresistance, while retained or elevated PLK2 activity correlates with improved treatment response in specific cancer settings.

Usage Information

Application

WB, IP

Dilution

WB	IP
1:1000	1:200

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

78 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

References

https://pubmed.ncbi.nlm.nih.gov/21382555/
https://pubmed.ncbi.nlm.nih.gov/23983262/

PLK2 Antibody [M21F17]

Biological Description

Usage Information

References

Application Data