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AB102108

Recombinant human PLK2 protein

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(1 Publication)

Recombinant human PLK2 protein is a Human Full Length protein, in the 1 to 685 aa range, expressed in Baculovirus infected Sf9 cells, with >85%, suitable for SDS-PAGE, FuncS.

View Alternative Names

SNK, PLK2, Serine/threonine-protein kinase PLK2, Polo-like kinase 2, Serine/threonine-protein kinase SNK, Serum-inducible kinase, PLK-2, hPlk2, hSNK

4 Images
Functional Studies - Recombinant human PLK2 protein (AB102108)
  • FuncS

Unknown

Functional Studies - Recombinant human PLK2 protein (AB102108)

The specific activity of PLK2 (ab102108) was determined to be 11 nmol/min/mg as per activity assay protocol

Functional Studies - Recombinant human PLK2 protein (AB102108)
  • FuncS

Unknown

Functional Studies - Recombinant human PLK2 protein (AB102108)

The specific activity of ab102108 was determined to be 13 nmol/min/mg.

SDS-PAGE - Recombinant human PLK2 protein (AB102108)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human PLK2 protein (AB102108)

ab102108 was determined to be >85% pure by densitometry. The predicted molecular weight is 106 kDa.

SDS-PAGE - Recombinant human PLK2 protein (AB102108)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PLK2 protein (AB102108)

SDS PAGE analysis of ab102108

Key facts

Purity

>85% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Active

Accession

Q9NYY3

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.307% Glutathione, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00292% EDTA, 0.00174% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Specific actvity is 13 nmol/min/mg.

ab91090 (Cow Casein full length protein) can be utilized as a substrate for assessing Kinase activity

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"106 kDa","actualMolecularWeight":null,"aminoAcidEnd":685,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9NYY3","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Specifications

Form

Liquid

Additional notes

ab102108 is >85% pure as measured by densitometry. Affinity purified.

General info

Function

Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling : required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CPAP and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.

Post-translational modifications

Catalytic activity is enhanced by phosphorylation of Thr-239.

Subcellular localisation

Cytoskeleton

Product protocols

Target data

Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling : required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CPAP and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.
See full target information PLK2

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Neuron 111:4006-4023.e10 PubMed38128479

2023

Serine-129 phosphorylation of α-synuclein is an activity-dependent trigger for physiologic protein-protein interactions and synaptic function.

Applications

Unspecified application

Species

Unspecified reactive species

Leonardo A Parra-Rivas,Kayalvizhi Madhivanan,Brent D Aulston,Lina Wang,Dube Dheeraj Prakashchand,Nicholas P Boyer,Veronica M Saia-Cereda,Kristen Branes-Guerrero,Donald P Pizzo,Pritha Bagchi,V S Sundar,Yong Tang,Utpal Das,David A Scott,Padmini Rangamani,Yuki Ogawa, Subhojit Roy
View all publications

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