Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Amino Acid > Kinesin

Kinesin

Kinesins are a family of motor proteins that use the energy from ATP hydrolysis to power their movement along microtubules.
They play a key role in intracellular transport, cargo movement, and cell division.
PubCompare.ai's AI-driven platform can help optimze your Kinesin research by locating the best protocols from literature, preprints, and patents, enhancing reproducibility and accuarcy to ensure you find the most reliable and effective methods for your Kinesin studies.
Unlock data-driven insights and take your Kinesin research to new heights.

Most cited protocols related to «Kinesin»

1
Imaging Kinesin Dynamics in C. elegans
Cited 36 times
Microscopy images were acquired using a custom-built epi-illuminated wide-field fluorescence microscope operated by a MicroManager software interface (μManager, MicroManager 1.4, www.micromanager.org; Edelstein et al. 2014 ) and built around an inverted microscope body (Eclipse Ti; Nikon, Amsterdam, Netherlands) fitted with a 60× water-immersion objective (CFI Plan Apo IR 60× water immersion, numerical aperture 1.27; Nikon). Excitation light was provided by a diode-pumped solid-state laser (Calypso 50, 491 nm; Cobolt, Solna, Sweden). Images were captured with an electron-multiplying charge-coupled device camera (iXon 897; Andor, Belfast, UK). One camera pixel corresponded to 92 nm × 92 nm in the image plane.
The C. elegans strain expressing EGFP-tagged OSM-3 kinesin motor proteins (Snow et al. 2004 (link)) was a kind gift of Jonathan M. Scholey (University of California, Davis, Davis, CA). Fluorescence imaging in living C. elegans was performed by anesthetizing adult worms (maintained at 20°C) in M9 containing 5 mM levamisole (tetramisole hydrochloride, L9756; Sigma-Aldrich, St. Louis, MO) and immobilizing them between a 2% agarose pad and a coverslip. Samples were imaged at room temperature (21°C) at 152 ms/frame.
Mangeol P., Prevo B, & Peterman E.J. (2016). KymographClear and KymographDirect: two tools for the automated quantitative analysis of molecular and cellular dynamics using kymographs. Molecular Biology of the Cell, 27(12), 1948-1957.
Publication 2016
Adult Electrons Fluorescence Helminths Kinesin Levamisole Light Light Microscopy Medical Devices Microscopy Microscopy, Fluorescence OSM-3 protein, C elegans Reading Frames Sepharose Snow Somatotype Strains Submersion Tetramisole thiacloprid
2
Liver Lipid Droplet Dynamics Regulation
Cited 14 times
See SI Appendix for detailed information. Reagents were purchased from Sigma-Aldrich unless otherwise mentioned. All animal protocols were approved by the Institutional Animal Ethics Committee (IAEC) formulated by the Committee for the Purpose of Control and Supervision of Experiments on Animals (CPCSEA), India. For reagents, plasmids, cell culture, and animal procedures, see SI Appendix, Sections 1–3. LDs were prepared from rat liver by sucrose density gradient (SI Appendix, Sections 5 and 8) and assayed for in vitro motility (SI Appendix, Section 6). ALDs prepared using glyceryl trioleate and PC were incubated with liver lysate before centrifugation and Western blotting (SI Appendix, Section 15). Cells infected with adenoviral shRNA were separated into LDs and soluble and membrane fractions (SI Appendix, Section 16). Rats were injected with kinesin-1 shRNA plasmid complexed with jetPEI, and later with Triton WR-1339. Serum was prepared for TG estimation and fractionation of ApoB containing lipoproteins (SI Appendix, Sections 17 and 23). Cellular and secreted TG was measured by LC-MS (SI Appendix, Section 21). ApoB was measured in cells and in liver lysates by Western blotting after immunoprecipitation (SI Appendix, Section 22). Liver lysate was subjected to ultracentrifugation to prepare microsomes and the membrane proteins were isolated for substrate hydrolysis assay (SI Appendix, Sections 24 and 25). Huh7.5 cells were infected with adenoviral shRNA followed by transfection with HCV-JFH-1 RNA. Cells and media were used for RNA isolation and qRT-PCR (SI Appendix, Section 26). See details of statistical analysis in SI Appendix, Section 27.
Rai P., Kumar M., Sharma G., Barak P., Das S., Kamat S.S, & Mallik R. (2017). Kinesin-dependent mechanism for controlling triglyceride secretion from the liver. Proceedings of the National Academy of Sciences of the United States of America, 114(49), 12958-12963.
Publication 2017
Adenoviruses Albinism-Deafness Syndrome Animals APOB protein, human Biological Assay Cell Culture Techniques Cells Centrifugation Fractionation, Chemical Hydrolysis Immunoprecipitation Institutional Ethics Committees isolation Kinesin Lipoproteins Liver Membrane Proteins Microsomes Plasmids Rattus norvegicus Serum Short Hairpin RNA Sucrose Supervision Tissue, Membrane Transfection Triolein Triton WR-1339 Ultracentrifugation
3
Modeling Kinesin Motor Dynamics
Cited 11 times

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2008
Dietary Supplements Kinesin Kinetics Motility, Cell
4
Microtubule Preparation and Stabilization
Cited 10 times

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2017
Buffers Cytoskeleton Kinesin Microscopy Molar Pharmaceutical Preparations Pigs Polymerization Taxol Tubulin Vitrification zampanolide
5
Microtubule Immobilization and Assay Preparation
Cited 9 times
The procedure below describes how to attach MTs to the glass cover slip and block the remaining surface to prevent unwanted adsorption of microspheres during subsequent optical trapping experiments (Fig. 9). At the near-neutral pH of most assay buffers, MTs have negative surface charge (especially at the C-terminal, glutamate-rich tubulin “E-hook” with which kinesin interacts) [51 (link)-54 (link)], whereas aminosilanized surfaces (pKa = 7-10 [55 , 56 (link)]) are protonated and thus positively charged. The MTs are thus rapidly adsorbed to the glass, whereupon they covalently bind the formyl groups left from previous glutaraldehyde treatment. During the MT incubation, reagents for the desired assay should be prepared (e.g., molecular motors bound to optical trapping beads in the presence of ATP; see Chapter 10). Following blocking with β-casein, the reagents are introduced to the flow chamber, the chamber ends are sealed, and the sample is taken to the microscope for the experiment.
Prepare the following freshly at the beginning of a set of experiments:

“BRB/Tx”: 350 μL of BRB80, 0.5 μL of 10 mM paclitaxel. Keep at room temperature.

Blocker: 156 μL of BRB/Tx, 14 μL of 25 mg/mL β-casein. Keep at room temperature.

“MT30”: 0.5 μL MT stock (10 mg/mL), 14.5 μL BRB/Tx (i.e., 30× dilution). Keep at room temperature and protect from the light (can be used for several days).

Do the following for each experiment:

Mix the MT30 suspension gently to evenly distribute the MTs. Add 0.5–0.8 μL MT30 (depending on the desired MT density on the cover slip) to 10 μL BRB/Tx. Flow this into a glutaraldehyde-treated flow chamber, using a piece of filter paper (seeFig. 5g) waiting on the opposite end in order to get very good flow through the chamber (this aligns the MTs with the chamber’s long axis) (seeNote 36 regarding the direction of flow).

Incubate the MTs in the chamber for 20–30 s and flush the chamber with 40 μL of BRB/Tx. Incubate 20 min or longer (seeNotes 46 and 47).

During the MT incubation, prepare the reagents for the main assay (see, e.g., Chapter 10 for a protocol to measure kinesin force generation), timed so that all incubations end at approximately the same time.

About 1 min before the end of the incubations, flush the flow chamber with 40 μL of Blocker and leave it to incubate.

Flow the assay solution into the flow chamber. Dry the ends with a Kimwipe, wiping away from the center of the chamber and taking care not to suck solution out of the chamber itself. Seal the chamber with vacuum grease as shown in Fig. 5h (seeNote 48). Avoid getting any grease on the surface of the cover slip that will contact the objective. When finished, wipe away any excess grease (seeNote 49).

Nicholas M.P., Rao L, & Gennerich A. (2014). Covalent Immobilization of Microtubules on Glass Surfaces for Molecular Motor Force Measurements and Other Single-Molecule Assays. Methods in molecular biology (Clifton, N.J.), 1136, 137-169.
Publication 2014
Adsorption Biological Assay Buffers Caseins Epistropheus Flushing Glutamate Glutaral Kinesin Light Microscopy Microspheres Paclitaxel Phocidae Strains Technique, Dilution Tubulin Vacuum

Most recents protocols related to «Kinesin»

1
Recombinant Leishmania Antigens Evaluation
The recombinant antigens, K28, K39, K18, and KR95, were purchased from Infectious Disease Research Institute (IDRI), Seattle, United States. To better evaluate the recombinant antigens K18 and KR95, the already known rK28 and rK39 proteins were employed.
rK39 (L. infantum—syn. chagasi) is part of a large protein kinesin-related (Lc-Kin), containing 298 amino acids and has a molecular mass of 38.9 kD [15 (link)].
rK28 (L. donovani) is a fusion polyprotein comprising HASPB1 (L. infantum K26 homolog), LdK39 (L. infantum K39 homolog), and HASPB2 (L. infantum K9 homolog) and has a molecular mass of 28.33 [19 (link)].
rKR95 (L. donovani) is a kinesin-related protein with a molecular mass of 95 kD, presenting 100% identity with L. infantum [28 (link)].
rK18 (L. infantum—syn. chagasi) is a tandem repeat hypothetical protein (also known as rTR18) with a molecular mass of 18 kD, presenting 100% identity with L. donovani [29 (link)].
Fujimori M., Valencia-Portillo R.T., Lindoso J.A., Celeste B.J., de Almeida R.P., Costa C.H., da Cruz A.M., Druzian A.F., Duthie M.S., Fortaleza C.M., de Oliveira A.L., Paniago A.M., Queiroz I.T., Reed S., Vallur A.C., Goto H, & Sanchez M.C. (2023). Recombinant protein KR95 as an alternative for serological diagnosis of human visceral leishmaniasis in the Americas. PLOS ONE, 18(3), e0282483.
Publication 2023
Amino Acids Antigens Communicable Diseases Kinesin Polyproteins Proteins Staphylococcal Protein A Tandem Repeat Sequences
2
Single-molecule kinesin motility assay
For Kif5B stepping assays, 0.2 nM Kif5B‐EGFP in kinesin motility buffer (BRB80, 10 μM Paclitaxel, 10 mM dithiothreitol, 20 mM D‐glucose, 0.5 mg/ml casein, 1 mM Mg‐ATP, 220 μg/ml glucose oxidase and 20 μg/ml catalase) were injected into the flow cell. Fluorescent images of single molecules were acquired at five frames per second for at least 1 min. Detailed acquisition information is indicated in the figure legends.
Motility parameters such as the interaction times, run length and velocities of Kif5B were determined by individually tracking the movement of single Kif5B‐EGFP molecules with the tracking software FIESTA (Ruhnow et al, 2011 (link)). The run length and interaction time were expressed as survival probability, determined by the Kaplan–Meier estimator in MATLAB (The MathWorks, Natick, MA, USA) and statistically compared as hazard ratios in JMP (Cary, NC, USA) as described previously (Henrichs et al, 2020 (link)). Kaplan–Meier analysis is a non‐parametric statistical test to estimate the survival function from lifetime data taking into account “censored events” that terminate due to causes unrelated to the kinesin walking mechanism (Ruhnow et al, 2017 (link)). Those events are processive runs prematurely terminated when Kif5B‐EGFP reaches microtubule ends, or move in‐ or out of the field of view. Including these events is important, as otherwise the analysis would be biased against long‐distance runs of kinesin molecules.
Using Kaplan–Meier analyses, thus, minimises the impact of possible variations in microtubule lengths (Ruhnow et al, 2017 (link)). Given that, in addition, we used microtubule sets of similar length distributions for our analyses (Fig EV4B) we can confidently exclude an influence of the microtubule lengths on the observed Kif5B‐EGFP run lengths and interaction times.
Genova M., Grycova L., Puttrich V., Magiera M.M., Lansky Z., Janke C, & Braun M. (2023). Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins. The EMBO Journal, 42(5), e112101.
Publication 2023
Biological Assay Buffers Caseins Catalase Cells Dithiothreitol Glucose KIF5B protein, human Kinesin Microtubules Motility, Cell Movement Oxidase, Glucose Paclitaxel Reading Frames
3
Microtubule Stabilization for Tau Binding
For Tau binding experiments, microtubules were polymerised in the presence of the slowly hydrolysable GTP‐analogue GMPCPP (Guanosine‐5′‐[(α,β)‐methyleno]triphosphate; Jena Bioscience NU‐405). Tubulin from murine brains was mixed with 1.25 mM GMPCPP and 1.25 mM MgCl2 to final concentrations of 4 μM in BRB80, and incubated for 3–5 h at 37°C. The polymerised microtubules were pelleted by centrifugation at 18,000 × g for 30 min. The supernatant was discarded, and pellets were resuspended in 100 μl of warm (37°C) BRB80.
For Tau‐envelope formation, kinesin stepping assays and microtubule severing, Taxol‐stabilised microtubules were prepared in BRB80 following a previously described protocol (Nitzsche et al, 2010 (link); Braun et al, 2011 (link)). We added 1.25 μl of the polymerisation mixture (25% DMSO, 20 mM MgCl2, 5 mM GTP in BRB80) to 5 μl of 4 mg/ml porcine tubulin. Microtubules were polymerised for 30 min at 37°C. Following centrifugation for 30 min at 18,000 × g and room temperature, the microtubule pellets were resuspended in 100 μl BRB80 containing 10 μM Taxol (Paclitaxel; Sigma‐Aldrich T7191).
GMPCPP‐ and Taxol‐stabilised microtubules were stored at room temperature and used for several days.
Genova M., Grycova L., Puttrich V., Magiera M.M., Lansky Z., Janke C, & Braun M. (2023). Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins. The EMBO Journal, 42(5), e112101.
Publication 2023
5'-guanylylmethylenebisphosphonate Biological Assay Brain Centrifugation Guanosine Kinesin Magnesium Chloride Microtubules Mus Paclitaxel Pellets, Drug Pigs Polymerization Sulfoxide, Dimethyl Taxol triphosphate Tubulin
4
Microscopic Imaging of Moss Chloronema
P. patens chloronema was observed using the MT marker (PpGCP4p::GFP–tubulin) (Kozgunova & Goshima, 2019 (link)), the dual-color marker of MT and nucleus (PpGCP4p::GFP–tubulin and 7113p::histone H2B–mRFP) (Kozgunova & Goshima, 2019 (link)), or Pp-Kinesin-12IIc and MT (Pp-Kinesin-12IIc–Citrine and PpACTp::mCherry–tubulin) (Miki et al, 2014 (link)).
For the PD-180970 experiment, chloronema tissues expressing MT marker cultured on a cellophane-laid BCDAT plate for 6 d were sonicated in a BCD liquid medium containing 10 μM oryzalin, 10 μM PD-180970, or 0.5% DMSO, followed by incubation for 30 min. The tissues were introduced into microfluidic devices and immediately observed (Kozgunova & Goshima, 2019 (link)). The images were acquired with an inverted microscope (Ti, 100 × 1.45 NA lens; Nikon) equipped with a spinning-disk confocal unit (CSU-X1; Yokogawa), 488- and 561-nm laser lines (LDSYS-488/561-50-YHQSP3, Pneum), and an electron-multiplying charge-coupled device camera (ImagEM; Hamamatsu) at 2.5-μm z-intervals. The microscope was controlled using NIS-Elements.
For PP2 experiments, chloronema tissues were cultured in six-well glass-bottom dishes or 35-mm dishes in a BCD agarose medium for 5–7 d (Yamada et al, 2016 (link)). Water containing 10 μM PP2 or 0.5% DMSO was directly applied to the dishes, and the mosses were incubated for 30 min before observation. High-resolution live-cell imaging of the Pp-Kinesin-12IIc/MT marker was performed using the same microscope described above. Long-term imaging of MT/histone markers was performed with a wide-field microscope (TE2000, 10 × 0.45 NA lens; Nikon) equipped with a CMOS camera (ZYLA-4.2P-USB3; Andor) and a Nikon Intensilight Epi-fluorescence illuminator, which was controlled by iQ software.
Kimata Y., Yamada M., Murata T., Kuwata K., Sato A., Suzuki T., Kurihara D., Hasebe M., Higashiyama T, & Ueda M. (2023). Novel inhibitors of microtubule organization and phragmoplast formation in diverse plant species. Life Science Alliance, 6(5), e202201657.
Publication 2023
Cell Nucleus Cellophane Cells Chronic multifocal osteomyelitis Electrons Fluorescence Histone H2b Histones Hyperostosis, Diffuse Idiopathic Skeletal Kinesin Lens, Crystalline Medical Devices Microchip Analytical Devices Microscopy Mosses oryzalin PD 180970 Pneumonia Sepharose Sulfoxide, Dimethyl Tissues Tubulin
5
Phosphoproteomics of Synchronized BY-2 Cells
For phosphoproteomics, BY–GTRC cells at 7 d after transfer to fresh medium were synchronized at the DNA replication stage (synthesis [S] phase) as described previously (Nagata & Kumagai, 1999 (link); Kumagai-Sano et al, 2006 (link)). The cells were cultured in the presence of PD-180970, PD-173955-Analog1, PP2, or PP3 for 8–9 h. After confirming that most cells started mitosis using an upright microscope (AxioImager A2; Zeiss), total proteins were extracted using cell lysis buffer (50 mM Tris–HCl [pH 8.0], 150 mM NaCl, 1% [vol/vol] Triton X-100, 25 μM MG-132, and cOmplete Mini Protease Inhibitor Cocktail [Roche]). After the extraction of crude proteins and trypsin digestion, peptides were purified using an immobilized metal ion affinity chromatography column or a sequential enrichment of immobilized metal affinity chromatography column, both of which specifically absorb phosphopeptides. Their amino acid sequences were determined using a high-sensitivity nanoLC-MS/MS system, as previously described (Ohkubo et al, 2021 (link)).
The protein sequences of BY-2 cells were predicted based on the transcriptome (RNA-seq) data, which have been previously reported (Kozgunova et al, 2016 (link)). Each of the transcript data was converted to an amino acid sequence, and a total of 50,171 protein sequences (coded from NtBYT000000.000 to NtBYT078147.000 in Supplemental Data 1) were used as a reference database to map the identified phosphopeptides by MASCOT search to determine the corresponding proteins. Identified proteins and their homologous proteins were aligned using Clustal Omega software (https://www.ebi.ac.uk/Tools/msa/clustalo/). Predictions of the MT-binding region in MAP70 proteins have been previously reported (Korolev et al, 2005 (link)). Kinesin motor domains and coiled-coil domains in PAKRP1 and PAKRP1L were predicted using UniProt (https://www.uniprot.org).
Kimata Y., Yamada M., Murata T., Kuwata K., Sato A., Suzuki T., Kurihara D., Hasebe M., Higashiyama T, & Ueda M. (2023). Novel inhibitors of microtubule organization and phragmoplast formation in diverse plant species. Life Science Alliance, 6(5), e202201657.
Publication 2023
Amino Acid Sequence Anabolism Buffers Cells Chromatography, Affinity Digestion DNA Replication Hypersensitivity Kinesin Metals MG 132 Microscopy Mitosis PD 173955 PD 180970 Peptides Phosphopeptides Protease Inhibitors Proteins RNA-Seq Sodium Chloride Somatostatin-Secreting Cells Tandem Mass Spectrometry Transcriptome Triton X-100 Tromethamine Trypsin

Top products related to «Kinesin»

1
Sephadex g 25 by GE Healthcare
Sourced in United States, Sweden, United Kingdom, Germany, Japan
Sephadex® G-25 is a gel filtration medium used in size exclusion chromatography. It is a cross-linked dextran-based material that separates molecules based on their size and molecular weight. Sephadex® G-25 is commonly used for desalting, buffer exchange, and sample clean-up applications.
2
Axio imager m2 microscope by Zeiss
Sourced in Germany, United States, France, Canada, United Kingdom
The Axio Imager M2 is a high-performance microscope designed for advanced imaging and analysis. It features a stable and ergonomic design, offering a range of optical and illumination options to suit various applications. The microscope is equipped with advanced imaging capabilities, ensuring high-quality data acquisition and precise results.
3
Matlab by MathWorks
Sourced in United States, United Kingdom, Germany, Canada, Japan, Sweden, Austria, Morocco, Switzerland, Australia, Belgium, Italy, Netherlands, China, France, Denmark, Norway, Hungary, Malaysia, Israel, Finland, Spain
MATLAB is a high-performance programming language and numerical computing environment used for scientific and engineering calculations, data analysis, and visualization. It provides a comprehensive set of tools for solving complex mathematical and computational problems.
4
Nocodazole by Merck Group
Sourced in United States, Germany, United Kingdom, Japan, Sao Tome and Principe, Canada, China, Switzerland, France, Poland, Macao, Australia
Nocodazole is a synthetic compound that acts as a microtubule-destabilizing agent. It functions by binding to and disrupting the polymerization of microtubules, which are essential components of the cytoskeleton in eukaryotic cells. This property makes Nocodazole a valuable tool in cell biology research for studying cell division, cell motility, and other cellular processes that rely on the dynamics of the microtubule network.
5
Taxol by Merck Group
Sourced in United States, Germany, Canada, United Kingdom, China
Taxol is a laboratory product manufactured by Merck Group. It is a complex organic compound used in various research and analysis applications. The core function of Taxol is to facilitate the stabilization of microtubules, which are essential structural components within cells.
6
Lipofectamine 2000 by Thermo Fisher Scientific
Sourced in United States, China, Germany, United Kingdom, Canada, Japan, France, Italy, Switzerland, Australia, Spain, Belgium, Denmark, Singapore, India, Netherlands, Sweden, New Zealand, Portugal, Poland, Israel, Lithuania, Hong Kong, Argentina, Ireland, Austria, Czechia, Cameroon, Taiwan, Province of China, Morocco
Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
7
Monastrol by Merck Group
Sourced in United States
Monastrol is a small molecule compound that selectively inhibits the mitotic kinesin Eg5, an essential motor protein required for the formation and function of the bipolar mitotic spindle during cell division. It is used as a research tool to study mitosis and cell division in various biological systems.
8
Neutravidin by Thermo Fisher Scientific
Sourced in United States, Germany, Switzerland, Israel
NeutrAvidin is a protein derived from avidin that binds to biotin with high affinity. It is commonly used in biotechnology applications as a tool for the detection, purification, and immobilization of biotinylated molecules.
9
Paraformaldehyde (pfa) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, France, Macao, Australia, Canada, Sao Tome and Principe, Japan, Switzerland, Spain, India, Poland, Belgium, Israel, Portugal, Singapore, Ireland, Austria, Denmark, Netherlands, Sweden, Czechia, Brazil
Paraformaldehyde is a white, crystalline solid compound that is a polymer of formaldehyde. It is commonly used as a fixative in histology and microscopy applications to preserve biological samples.
10
Mono q column by GE Healthcare
Sourced in United Kingdom, United States, Sweden
The Mono Q column is a high-performance ion exchange chromatography column designed for the purification and separation of biomolecules. It features a strong anion exchange resin for the capture and fractionation of charged proteins, peptides, and other charged species.

More about "Kinesin"

Kinesins are a family of motor proteins that play a crucial role in cellular transport and division processes.
These molecular motors utilize the energy released from ATP hydrolysis to power their movement along microtubule tracks within the cell.
Kinesins are involved in a wide range of intracellular activities, including cargo transportation, organelle positioning, and spindle formation during cell division.
The study of kinesins has been greatly enhanced by the availability of various laboratory techniques and tools.
For instance, Sephadex® G-25 is a size-exclusion chromatography medium commonly used for the purification and separation of kinesin proteins.
The Axio Imager M2 microscope, equipped with fluorescence and differential interference contrast (DIC) capabilities, allows for the visualization and analysis of kinesin-mediated movements and interactions within the cellular environment.
Computational tools, such as MATLAB, have also proven invaluable in the analysis and modeling of kinesin dynamics, enabling researchers to gain deeper insights into the mechanistic aspects of these molecular motors.
Pharmacological agents like Nocodazole, which disrupts microtubule polymerization, and Taxol, which stabilizes microtubules, have been instrumental in studying the dependence of kinesin function on the integrity of the microtubule cytoskeleton.
In addition, techniques like Lipofectamine 2000-mediated transfection have facilitated the overexpression or knockdown of kinesin proteins, enabling researchers to investigate their roles in specific cellular processes.
Monastrol, a small-molecule inhibitor of the kinesin Eg5, has been widely used to study the involvement of kinesins in spindle assembly and cell division.
Other important tools and reagents include NeutrAvidin, a streptavidin derivative used for the immobilization and study of biotinylated kinesin proteins, and paraformaldehyde, a fixative commonly employed in the preparation of samples for microscopic examination of kinesin-related structures and interactions.
By leveraging these diverse experimental approaches and technologies, researchers can delve deeper into the intricate workings of kinesins, unraveling their fundamental roles in cellular processes and paving the way for potential therapeutic applications targeting kinesin-mediated pathways.