| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Serine/threonine-protein kinase PLK1;2.7.11.21;Polo-like kinase 1;PLK-1;Serine/threonine-protein kinase 13;STPK13;PLK1;PLK; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human PLK1 recombinant protein (Position: K86-N430). Human PLK1 shares 95.4% and 96.2% amino acid (aa) sequence identity with mouse and rat PLK1, respectively. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
This antibody is intended for detection of PLK1 (Serine/threonine-protein kinase PLK1) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.
Vendor notes: Boster Bio Anti-PLK1 Antibody Picoband® catalog # PB9500. Tested in WB applications. This antibody reacts with Human. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Antibody format: Rabbit Polyclonal Rabbit IgG
- Immunogen / epitope context: E.coli-derived human PLK1 recombinant protein (Position: K86-N430). Human PLK1 shares 95.4% and 96.2% amino acid (aa) sequence identity with mouse and rat PLK1, respectively. (reported region: K86-N430).
- Molecular weight context: reported MW: 68 kDa; calculated MW: 68255 MW
- Reactivity: Human
- Applications: WB
As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.
Biological background
Serine/threonine-protein kinase PLK1; Serine/threonine-protein kinase PLK1. 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. Functional note: 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, SGOL1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1 and WEE1. 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 SGOL1: required for spindle pole localization of isoform 3 of SGOL1 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 (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069). 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 (By similarity). . Reported localization: Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody. During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer kinetochore. Presence of SGOL1 and interaction with the phosphorylated form of BUB1 is required for the kinetochore localization. Localizes onto the central spindle by phosphorylating and docking at midzone proteins KIF20A/MKLP2 and PRC1. Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle. Expression/tissue context: Placenta and colon.
Research relevance and current trends
- Cancer: Researchers commonly examine how PLK1 (Serine/threonine-protein kinase PLK1) relates to this theme using model systems and orthogonal readouts.
- Cell Cycle: Researchers commonly examine how PLK1 (Serine/threonine-protein kinase PLK1) relates to this theme using model systems and orthogonal readouts.
- Cell Division: Researchers commonly examine how PLK1 (Serine/threonine-protein kinase PLK1) relates to this theme using model systems and orthogonal readouts.
Common research applications
- Western blotting: compare relative PLK1 (Serine/threonine-protein kinase PLK1) levels across conditions; band patterns may reflect isoforms and processing.
Notes for experimental interpretation
- Specificity notes: No cross reactivity with other proteins.
- Cross-reactivity: No cross-reactivity with other proteins
- Family / similarity context: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
- Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
- Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.
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