Anti-PLK1 Antibody Picoband® (monoclonal, 6D11)

Overview

Anti-PLK1 Antibody Picoband® (monoclonal, 6D11) is an antibody for PLK1 detection raised in Mouse (Monoclonal, clone Clone: 6D11, Mouse IgG2b), with reported reactivity: Human,Monkey. Commonly used in WB, IHC, Flow Cytometry, ELISA workflows.

Key elements and design rationale

• Target: PLK1 (polo like kinase 1); UniProt: P53350
• Antibody format: Mouse, Monoclonal, clone Clone: 6D11, Mouse IgG2b
• Molecular weight: 68 kDa, calculated 46659 MW
• Applications: WB, IHC, Flow Cytometry, ELISA

Vendor description (summary): Boster Bio Anti-PLK1 Antibody Picoband® (monoclonal, 6D11) catalog # M00182.

Biological background

Biological context: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning. Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage. Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope. Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock. Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF (BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression. Regulates mitotic progression by phosphorylating RIOK2.

Expression and localization notes: cellular localization: Centrosome. Spindle. Nucleus. Kinetochore. Midbody., tissue context: Placenta and colon..

Common research applications

• Western blotting (WB): Compare PLK1 levels across samples and conditions using appropriate loading and biological controls.
• Immunohistochemistry (IHC): Evaluate spatial distribution of PLK1 in tissue sections, considering fixation and antigen retrieval effects.
• Flow cytometry: Quantify PLK1-positive populations in single-cell suspensions with appropriate gating and controls.
• ELISA: Use antibody-based detection formats to assess antigen presence or binding in plate-based assays.

Notes for experimental interpretation

• Account for isoforms, post-translational modifications, and sample-specific processing that can shift apparent molecular weight or epitope accessibility.
• Use positive/negative biological controls where possible (e.g., known-expressing cells/tissues, knockdown/knockout models) and include appropriate secondary-only/isotype controls for imaging workflows.

Additional product notes (from provided fields)

• Specificity: No cross reactivity with other proteins.
• Background: Serine/threonine-protein kinase PLK1, also known as polo-like kinase 1 (PLK-1) or serine/threonine-protein kinase 13 (STPK13), is an enzyme that in humans is encoded by the PLK1 (polo-like kinase 1) gene. Plk1 is an early trigger for G2/M transition. It supports the functional maturation of the centrosome in late G2/early prophaseand establishment of the bipolar spindle. Also, Plk1 phosphorylates and activates cdc25C, a phosphatase that dephosphorylates and activates the cyclinB/cdc2 complex. Studies have shown that the loss of PLK1 expression can inducepro-apoptotic pathways and inhibit growth. Based on yeast and murine studies of meiosis, human PLK1 may also have a regulatory function in meiosis.
• Cross reactivity: No cross-reactivity with other proteins.
• Cellular localization: Centrosome. Spindle. Nucleus. Kinetochore. Midbody.
• Tissue details: Placenta and colon.
• Research category: Calcium Channels,Calcium Signaling,Cancer,Cancer Metabolism,Energy Transfer Pathways,Integration Of Energy,Integration Of Energy Metabolism,Metabolic Signaling Pathway,Metabolic Signaling Pathways,Metabolism,Neuroscience,Neurotransmission,Pathways and Processes,Signal Transduction,Signaling Pathway

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