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LB-100

LB-100 is a small-molecule inhibitor that targets the serine/threonine protein phosphatase 2A (PP2A) enzyme.
PP2A is a key regulator of cellular processes and is involved in the pathogenesis of various diseases, including cancer.
LB-100 has shown promising preclinical results in inhibiting tumor growth and enhancing the efficacy of other anticancer therapies.
Reserchers can utilize PubCompare.ai to optimize their LB-100 research protocols, identify the most effective approaches, and advance their studies on this importatnt therapeutic target.

Most cited protocols related to «LB-100»

Overexpression and Purification of Phosphorylated GST-CaM

Cited 18 times

For overexpression of GST-CaM incorporating phosphoserine, DH10B ΔserB or C321(DE3) ΔserB E. coli cells were transformed by electroporation with pRSF and pKW vectors, and recovered in 1 ml SOB medium for one hour at 37°C prior to aliquoting to 100 ml LB-KC (LB media with 25 μg/ml kanamycin, and 17.5 μg/ml chloramphenicol) and incubated overnight (37°C, 250 r.p.m., 16 h). The overnight culture was diluted to OD₆₀₀=0.1 in LB-KC. At OD₆₀₀=0.5, IPTG (1 mM final concentration) and phosphoserine (2 mM) were added to the culture. The culture was incubated (37°C, 250 r.p.m.) for 5 h, pelleted (3,000g, 10 min, 4°C) and washed twice with 1 ml PBS. The overexpressed proteins were purified using the glutathione affinity chromatography. Cell pellets were resuspended in 1 ml of BugBuster Protein Extraction Reagent (Novagen) (supplemented with 1× protease inhibitor cocktail tablet (Roche), 1 mg ml⁻¹ lysozyme (Sigma), 1 mg ml⁻¹ DNase I (Sigma)) and lysed (25°C, 250 r.p.m., 1 h). The lysate was clarified by centrifugation (25,000g, 30 min, 4°C). GST containing proteins from the lysate were bound in batch (1 h, 4°C) to 70 μl of glutathione sepharose beads (GE Healthcare). Beads were washed 4 times with 1 ml PBS prior to elution by heating in 1× NuPAGE LDS sample buffer (Invitrogen, 95°C, 5 min) supplemented with 100 mM DTT. All samples were analysed on 4-12% Bis-Tris gels (Invitrogen) with BIO-RAD Low Range Molecular Weight Standard as marker. The gels were subsequently stained with Coomassie Blue (InstantBlue, Expedeon).

Rogerson D.T., Sachdeva A., Wang K., Haq T., Kazlauskaite A., Hancock S.M., Huguenin-Dezot N., Muqit M.M., Fry A.M., Bayliss R, & Chin J.W. (2015). Efficient genetic encoding of phosphoserine and its non-hydrolyzable analog. Nature chemical biology, 11(7), 496-503.

Publication 2015

Bistris Buffers Cells Centrifugation Chloramphenicol Chromatography, Affinity Cloning Vectors Coomassie blue Deoxyribonucleases Electroporation Escherichia coli Gels Glutathione Isopropyl Thiogalactoside Kanamycin LB-100 Muramidase Pellets, Drug Phosphoserine Proteins Sepharose SERPINA1 protein, human Tablet

Generation of Klebsiella pneumoniae Mutants

Cited 13 times

Lambda Red mutagenesis was performed as previously described (15 (link)). To make electrocompetent cells, K. pneumoniae containing the pKD46 plasmid (15 (link)), modified to encode spectinomycin resistance (a gift from Chris Alteri), was cultured overnight in LB broth containing spectinomycin at 30°C with shaking. The following day, cultures were diluted 1:100 in LB broth with spectinomycin and 50 mM l-arabinose and cultured at 30°C until reaching a reading of optical density at 600 nm (OD₆₀₀) of 0.5 to 0.6 (approximately 4 h). Cultures were placed on ice for at least 30 min and centrifuged in sterile cold bottles at 8,000 × g for 15 min at 4°C. The supernatant was decanted, and bacteria were serially washed and centrifuged in ice-cold sterile volumes of 50 ml 1 mM HEPES at pH 7.4 (Invitrogen, Carlsbad, CA), 50 ml distilled water (dH₂O), and 20 ml 10% glycerol. Pellets were resuspended in ice-cold sterile 10% glycerol at a final density of 2 × 10¹⁰ to 3 × 10¹⁰ CFU/ml and stored at −80°C in 50-µl aliquots.
To generate null mutants, E. coli BW25141 containing the pKD4 plasmid was cultured overnight in LB broth containing 50 µg/ml kanamycin (MP Biomedicals, Santa Ana, CA) at 30°C. The pKD4 plasmid was isolated using a Spin Miniprep kit (Qiagen, Valencia, CA). Oligonucleotide primers were then designed with 60-bp homology flanking the region targeted for deletion added to 5′ ends of P1 and P2 sites of the pKD4 kanamycin resistance cassette (see Table S2 in the supplemental material). The targeting fragment was generated by PCR consisting of 95°C for 5 min; 30 cycles of 95°C for 1 min, 58°C for 1 min, and 72°C for 1 min; and 72°C for 5 min. PCR products were pooled and purified using a Qiagen PCR purification kit. PCR products were digested overnight at 37°C with DpnI, and 10 µl was added to the electrocompetent pKD46 cells, gently mixed, and incubated on ice for 10 min. The mixture was electroporated using a 0.1-cm-gap cuvette (Fisher Scientific; catalog no. FB101) at 1.8 kV, 400 Ω, 25 µF, with a Bio-Rad Micropulser (Bio-Rad, Hercules, CA), and cells were recovered with SOC medium and incubated overnight at 30°C with shaking in sterile culture tubes. Next, cells were spun down, resuspended in LB broth, plated onto LB broth plates containing kanamycin, and incubated at 37°C overnight. Transformants were restreaked on LB agar and confirmed by colony PCR using flanking primers (see Table S2).
To complement the rfaH and copA mutants, PCR products containing the open reading frame and upstream sequence (see Table S2 in the supplemental material) were inserted into pCR 2.1 by TOPO TA cloning (Life Technologies, Carlsbad, CA) and transferred to pACYC184 by ligation after digestion with Xbal and HindIII. The resulting complementation plasmid or pACYC184 alone was introduced into WT or mutant K. pneumoniae by electroporation.

Bachman M.A., Breen P., Deornellas V., Mu Q., Zhao L., Wu W., Cavalcoli J.D, & Mobley H.L. (2015). Genome-Wide Identification of Klebsiella pneumoniae Fitness Genes during Lung Infection. mBio, 6(3), e00775-15.

Publication 2015

Agar Arabinose Autosomal Recessive Polycystic Kidney Disease Bacteria Cells CHOP regimen Cold Temperature Deletion Mutation Digestion Electroporation Escherichia coli Glycerin HEPES Kanamycin Kanamycin Resistance Klebsiella pneumoniae LB-100 Ligation Mutagenesis Oligonucleotide Primers Pellets, Drug Plasmids Spectinomycin Sterility, Reproductive Topotecan

Bacterial Growth and ATP Determination

Cited 10 times

Bacteria were cultured in LB broth at 37°C overnight with shaking at 225 rpm. Overnight cultures were diluted 1:100 in fresh LB broth and cultured at 37°C with shaking. Aliquots of cultures were taken after 3, 6, 9, and 24 hours of incubation, and OD_{600 nm} was measured at each time point. Bacterial cultures were then centrifuged at 16,100 × g for 5 min. Culture supernatant was transferred to a fresh tube and stored at −80°C until assayed.
ATP level in bacterial supernatant was determined using BacTiter-Glo™ Microbial Cell Viability Assay Reagent (Promega, Madison, WI). It is a luciferase – based assay and the ATP level is determined by measuring luminescence levels and comparing to an ATP standard curve. One hundred microliters of culture supernatant were mixed with an equal volume of BacTiter-Glo™ Microbial Cell Viability Assay Reagent in a 96-well opaque plate and incubated at room temperature for 5 min. After incubation, luminescence was read in a SpectraMax M2 plate reader (Molecular Devices, Sunnyvale, CA). ATP standard solutions were prepared using adenosine 5-triphosphate disodium salt hydrate (A2383, Sigma Aldrich, St. Louis, MO) and a standard curve using 10-fold dilutions of ATP standard solutions prepared in H₂O was included in each experiment. ATP concentrations in bacterial samples were determined by comparing to the ATP standard curve for each assay. LB, H₂O or buffer was included in all assays as the negative controls.
The ATP level in bacterial cells was determined similarly as described for the culture supernatant. Bacteria were cultured in LB broth with shaking at 37°C. After various culture periods, an aliquot of a culture was collected for measuring OD_600nm and for preparing bacterial extracts using the perchloric acid extraction method [14 (link)]. Two hundred microliters of bacterial culture were mixed with 100 μl of ice – cold 1.2 M perchloric acid and vortexed for 10 seconds. The mixture was incubated on ice for 15 min. and spun down at 16,100 × g for 5 min. at 4°C. Two hundred microliters of supernatant were transferred to a fresh tube and mixed with 100 μl of a neutralizing solution containing 0.72 M KOH and 0.16 M KHCO₃. The neutralized extract was then spun down at 16,100 × g for 5 min. and the supernatant was transferred to a fresh tube for use for theATP assay.

Mempin R., Tran H., Chen C., Gong H., Kim Ho K, & Lu S. (2013). Release of extracellular ATP by bacteria during growth. BMC Microbiology, 13, 301.

Publication 2013

Adenosine Triphosphate Bacteria Biological Assay Buffers Cell Survival Cold Temperature LB-100 Luciferases Luminescence Medical Devices Microbial Viability Neoplasm Metastasis Perchloric Acid potassium bicarbonate Promega Sodium Chloride Technique, Dilution

Heterodimeric CP Protein Purification

Cited 10 times

Synthetic genes containing the E. coli optimized nucleotide sequences for human S100A8 and S100A9 were obtained in the pJ201 vector from DNA 2.0 and subcloned into the NdeI and XhoI sites of pET41a (Supporting Information). A modified Quick-Change site-directed mutagenesis protocol (Stratagene) was employed to generate the CP mutants. The resulting pET41a-S100A8 and pET41a-S100A9 expression plasmids were transformed into chemically-competent E. coli BL21(DE3) cells. Cultures from single colonies were grown to saturation in LB media containing 50 μg/mL kanamycin (37 °C with agitation, t ~ 16 h), and freezer stocks were prepared by diluting the overnight cultures with an equal volume of 1:1 water/glycerol (sterile) and stored at −80 °C. For protein overexpression, over-night cultures were grown to saturation in LB media containing 50 μg/mL kanamycin (37 °C, 150 or 175 rpm, t ~ 16 h) and diluted 1:100 into fresh LB media containing 50 μg/mL kanamycin, incubated at 37 °C with shaking at 150 rpm, and induced with 500 μM IPTG at OD₆₀₀ ~ 0.6. The cultures were incubated at 37 °C for an additional 3–4 h (OD₆₀₀ ~ 1.5), and pelleted by centrifugation (4 200 rpm × 30 min, 4 °C). The cell pellets were transferred to pre-weighed 50-mL polypropylene centrifuge tubes, flash frozen in liquid N₂, and stored at −80 °C. The reconstitution and purification of heterodimeric CP and all mutants were performed making several modifications to literature procedures.^{10 (link), 25 (link), 37 (link)} Complete details for cloning, site-directed mutagenesis, protein overexpression and purification, protein storage and handling are provided as Supporting Information.

Brophy M.B., Hayden J.A, & Nolan E.M. (2012). Calcium Ion Gradients Modulate the Zinc Affinity and Antibacterial Activity of Human Calprotectin. Journal of the American Chemical Society, 134(43), 18089-18100.

Publication 2012

Base Sequence Cells Centrifugation Cloning Vectors Escherichia coli Freezing Glycerin Homo sapiens Isopropyl Thiogalactoside Kanamycin LB-100 Mutagenesis, Site-Directed Pellets, Drug Plasmids Polypropylenes Proteins Sterility, Reproductive Synthetic Genes

Quantifying A118 Biofilm Formation

Cited 9 times

A118 cells were cultured in LB broth with or without 0.2% HSA and incubated with agitation for 18 h at 37 °C. Overnight cultures were centrifuged at 5,000 rpm at 4 °C for 5 and cell pellets were washed twice with 1X PBS and then re-suspended in 1X PBS. Following, the optical density at 600 nm (OD₆₀₀) of each culture was adjusted to 0.9–1.1, vortexed and diluted 1:100 in LB broth before being plated in technical triplicate in a 96-well polystyrene micro-titer plate and being incubated at 37 °C for 24 h without agitation. The following day, the OD₆₀₀ (ODG) was measured using a micro-plate reader (SpectraMax M3 microplate/ cuvette reader with SoftMax Pro v6 software) to determine the total biomass. Wells were emptied with a vacuum pipette, washed three times with 1X phosphate-buffered saline (PBS) and stained with 1% crystal violet (CV) for 15 m. Excess CV was removed by washing three more with 1X PBS and the biofilm associated with the CV was solubilized in ethanol acetate (80:20) for 30 m. The OD₅₈₀ (ODB) was measured using a micro-plate reader and results were reported as the ratio of biofilm to total biomass (ODB/ODG). Experiments were performed in triplicate, statistical analysis (Mann-Whitney test) was performed using GraphPad Prism (GraphPad software, San Diego, CA, USA), and a P-value < 0.05 was considered significant.

Quinn B., Rodman N., Jara E., Fernandez J.S., Martinez J., Traglia G.M., Montaña S., Cantera V., Place K., Bonomo R.A., Iriarte A, & Ramírez M.S. (2018). Human serum albumin alters specific genes that can play a role in survival and persistence in Acinetobacter baumannii. Scientific Reports, 8, 14741.

Publication 2018

Acetate Biofilms Cells Ethanol LB-100 Pellets, Drug Phosphates Polystyrenes prisma Saline Solution Vacuum Violet, Gentian Vision

Most recents protocols related to «LB-100»

Combinatorially Complete scFv Library

To assemble the combinatorially complete library containing all 2¹⁶ = 65,536 variants, the scFv sequence was sectioned into five fragments of roughly equal length such that each fragment contained ≤5 mutations. Primers were designed to create all possible (≤2⁵) versions of each fragment by adding mutations, a Bsa-I cleavage site, and a 4 bp overhang unique to each fragment (Supplementary file 3). Fragments were amplified from the UCA860 sequence via PCR using Q5 Polymerase (NEB, Ipswich, MA, #M0491). The resulting fragments were purified using a 2× ratio of Aline beads (Aline Biosciences, Woburn, MA, #C-1003-5), overnight DpnI digestion at 37°C (NEB #R0176), and a second 2× ratio bead cleanup. The backbone vector was prepared by replacing the scFv sequence in the pCHA yeast display vector with a ccdb counter-selection marker. Equimolar amounts of each fragment were then pooled and assembled into the backbone vector at a 2:1 molar ratio via Golden Gate Assembly (Engler et al., 2008 (link); NEB #R3733). The assembly mix was then transformed into electrocompetent DH10B Escherichia coli in 5 × 25 uL cell aliquots (NEB #C3020). Each cell aliquot was recovered in 1 mL outgrowth media at 37°C for 1 hr and then transferred into 100 mL of molten LB (1% tryptone, 0.5% yeast extract, 1% NaCl, 100 g/L ampicillin [VWR # V0339], 0.4% SeaPrep agarose [VWR, Radnor, PA #12001-922]) in a 500 mL baffled flask. The bacteria–agar mixture was incubated at 4°C for 3 hr to gel the agar and was then incubated at 37°C for 16 hr. Each flask contained 1–2 million colonies (5–10 million colonies across five flasks; >100 times the library diversity) and was blended by shaking at 200 rpm for 1 hr. The cells were then pelleted by spinning at 3000 × g for 10 min, and plasmid DNA was extracted using the ZymoPURE II Plasmid Midiprep Kit (Zymo Research, Irvine, CA, #D4201).

Phillips A.M., Maurer D.P., Brooks C., Dupic T., Schmidt A.G, & Desai M.M. (2023). Hierarchical sequence-affinity landscapes shape the evolution of breadth in an anti-influenza receptor binding site antibody. eLife, 12, e83628.

Publication 2023

Agar Ampicillin Bacteria Cells Cloning Vectors Cytokinesis Digestion DNA Library Escherichia coli LB-100 Molar Mutation Oligonucleotide Primers Plasmids Saccharomyces cerevisiae Sepharose Sodium Chloride Vertebral Column

Glucose Assay of Bacterial Growth

Overnight cultures were subcultured at a 1:100 dilution in 50 ml of LB medium for 0 (without bacteria), 2, 4, and 6 hours. Supernatant was collected by centrifugation for glucose content using the CheKine Micro Glucose Assay Kit (KTB1300, Abbkine Scientific Co. Ltd., China). Briefly, 50 μl of supernatant was added to 1000 μl of o-toluidine reagent and vortexed. The mixture was heated in a boiling water bath for 8 min and cooled to room temperature in a cool water bath for 4 min. Then, 200 μl of each mixture was added to a 96-well plate, and absorbance at 630 nm was measured.

Jiang M., Su Y.B., Ye J.Z., Li H., Kuang S.F., Wu J.H., Li S.H., Peng X.X, & Peng B. (2023). Ampicillin-controlled glucose metabolism manipulates the transition from tolerance to resistance in bacteria. Science Advances, 9(10), eade8582.

Publication 2023

2-toluidine Bacteria Bath Biological Assay Centrifugation Glucose LB-100 Technique, Dilution

Expression and Purification of AceE and Mutants

For AceE and eight mutants’ protein expression and purification, a colony of DE3 containing recombinant plasmids pET-28a-aceE or each of the eight pET-28a-mutant genes was cultured in 5 ml of LB medium with ampicillin (100 μg/ml) at 37°C with shaking for 16 hours. The cultures were diluted in 1:100 to 500 ml of LB medium supplemented with ampicillin and incubated at 37°C until the OD₆₀₀ reached 0.5. Then, 0.1 mM isopropyl-β-d-thiogalactoside (IPTG) was added to induce the recombinant protein at 16°C for 12 hours. Bacteria were harvested by centrifugation at 8000g and resuspended in 0.01 mM (pH 7.4) phosphate-buffered saline (1 × PBS). The resulting cells were disrupted by high pressure (1.586 × 10⁺⁸ Pa) using a cell disruptor (Constant Systems Ltd., Daventry, UK), and supernatant was obtained by centrifugation at 8000g for 30 min at 4°C. The supernatant was applied onto a nickel-affinity column and incubated at 4°C for 2 hours. After protein binding, the column was washed with 10 volumes of washing buffer (1× PBS buffer with 5 mM imidazole) to remove unbound protein. Recombinant proteins were eluted with elution buffer (1× PBS buffer with 100 mM imidazole), respectively. Purity and concentration of recombinant proteins were analyzed and quantified by SDS–polyacrylamide gel electrophoresis and a bicinchoninic acid protein concentration determination kit (Beyotime, P0009).

Publication 2023

Ampicillin Bacteria bicinchoninic acid Buffers Cells Centrifugation Genes imidazole Isopropyl Thiogalactoside LB-100 Mutant Proteins Nickel Phosphates Plasmids Pressure Proteins Recombinant Proteins Saline Solution SDS-PAGE

Intracellular Iron Level Quantification

Cells were grown in LB medium overnight and subcultured with 1 : 100 ratio into LB medium to an OD₆₀₀ of ~0.4. Cells were harvested, and levels of intracellular Fe were monitored by ICP-MS. All samples were washed once with chelex-treated phosphate-buffered saline (PBS) buffer containing 1 mM EDTA and then twice with chelex-treated PBS. Cell pellets were resuspended in 400 µl of buffer 2 (1× chelex-treated PBS buffer, 75 mM NaN₃, 1 % Triton X-100) and incubated at 37 °C for 90 min to lyse the cells. Lysed samples were spun down by centrifugation and the total protein content was quantified using a Bradford assay. Then, samples were mixed with 600 µl buffer 4 [5 % HNO₃, 0.1 % (v/v) Triton X-100] and heated in a 95 °C sand bath for 30 min. The debris was removed by centrifugation and the total metal ions in the diluted samples were analysed by Perkin-Elmer ELAN DRC II ICP-MS. Gallium was used as an internal standard. (mean±se; n=3).

Steingard C.H., Pinochet-Barros A., Wendel B.M, & Helmann J.D. (2023). Iron homeostasis in Bacillus subtilis relies on three differentially expressed efflux systems. Microbiology, 169(1), 001289.

Publication 2023

Baths, Sand Biological Assay Buffers Cells Centrifugation chelex Edetic Acid Gallium Ions LB-100 Metals Pellets, Drug Phosphates Proteins Protoplasm Saline Solution Sodium Azide Triton X-100

Bacterial Growth and Biofilm Characterization

The growth curves were made following a previous study [50 (link)]. First, a single colony of bacteria was standardized to match a 0.5 McFarland followed by 1:100 dilution in LB broth at 37 °C with medium shaking. Then, 200 μL of the bacterial solution was taken out, and the optical density at 600 nm (OD₆₀₀) was measured every hour during the first 12 h. Finally, multiple t-test was used to compare growth at various time points.
Biofilm formation was assessed by the crystal violet staining method [51 (link)]. The strains were prepared into 1.0 × 10⁸ CFU/mL solution with PBS, diluted to 1:100 with LB broth, and cultured in a 96-well plate (3 parallel wells for each strain) at 37 °C for 24 h. The plate was then washed with PBS, stained with 1% crystal violet for 15 min, and then decolorized with 95% ethanol for 10 min. Absorbance was measured at OD₅₇₀. The classification standard followed the previous study [52 (link)]. Growth curves and biofilm assay were performed in triplicate.

Tang M., Li J., Liu Z., Xia F., Min C., Hu Y., Wang H, & Zou M. (2023). Clonal transmission of polymyxin B-resistant hypervirulent Klebsiella pneumoniae isolates coharboring blaNDM-1 and blaKPC-2 in a tertiary hospital in China. BMC Microbiology, 23, 64.

Publication 2023

Bacteria Biofilms Biological Assay Ethanol LB-100 Staining Strains Technique, Dilution Violet, Gentian Vision

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Lb 100 by Selleck Chemicals

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Ampicillin is a broad-spectrum antibiotic used in laboratory settings. It is a penicillin-based compound effective against a variety of gram-positive and gram-negative bacteria. Ampicillin functions by inhibiting cell wall synthesis, leading to bacterial cell lysis and death.

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The High-Capacity cDNA Reverse Transcription Kit is a laboratory tool used to convert RNA into complementary DNA (cDNA) molecules. It provides a reliable and efficient method for performing reverse transcription, a fundamental step in various molecular biology applications.

What is LB-100 and how does it work?

What are some common applications of LB-100?

LB-100 is primarily used in cancer research to investigate its potential as an anti-cancer agent. Researchers have studied its ability to inhibit tumor growth and improve the effectiveness of other cancer treatments. Additionally, LB-100 may have applications in the study of other diseases involving dysregulation of the PP2A pathway, such as Alzheimer's disease and neurological disorders.

How can PubCompare.ai help researchers working with LB-100?

PubCompare.ai allows researchers to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to LB-100 for their specific research goals. PubCompare.ai's AI-driven analysis can highlight key differences in protocol effectiveness, enabling researchers to choose the best option for reproducibility and accuracy in their LB-100 studies.

Are there any variations or different types of LB-100?

While LB-100 is the primary small-molecule inhibitor of PP2A, there may be related compounds or derivatives that researchers are exploring. However, the information available suggests that LB-100 is the most widely studied and characterized inhibitor in this class. Researchers should consult the literature and patents to stay up-to-date on any new variations or analogues of LB-100 that may emerge.

What are some common challenges in using LB-100 in research?

One potential challenge in using LB-100 is ensuring the optimal dosage and administration for the desired effect. Researchers may need to experiment with different concentrations and delivery methods to achieve the desired inhibition of PP2A and the resulting impact on cellular processes or disease models. Additionally, there may be considerations around the stability and solubility of LB-100 in different experimental conditions. Carefull planning and optimization of LB-100 protocols can help address these challenges.

More about "LB-100"

LB-100 is a promising small-molecule inhibitor that targets the serine/threonine protein phosphatase 2A (PP2A) enzyme, a key regulator of cellular processes involved in various diseases, including cancer.
This potent PP2A inhibitor has demonstrated impressive preclinical results in inhibiting tumor growth and enhancing the efficacy of other anti-cancer therapies.
Researchers can utilize cutting-edge tools like PubCompare.ai, an AI-driven platform, to optimize their LB-100 research protocols and identify the most effective approaches to advance their studies on this important therapeutic target.
By leveraging PubCompare.ai, researchers can effortlessly locate the best protocols from literature, preprints, and patents, and then use the AI-powered comparisons to pinpoint the most effective protocols and products for their LB-100 research.
In addition to LB-100, researchers may also employ a range of other laboratory equipment and reagents, such as the Infinite M200 Pro microplate reader, Synergy H1 multi-mode reader, TRIzol reagent for RNA extraction, the RNeasy Mini Kit for RNA purification, the QIAprep Spin Miniprep Kit for plasmid DNA extraction, and ampicillin for bacterial selection.
Protease inhibitor cocktails may also be utilized to preserve the integrity of proteins during experiments.
Furthermore, the High-Capacity cDNA Reverse Transcription Kit can be employed for the conversion of RNA to cDNA, a crucial step in various molecular biology techniques.
By combining the power of PubCompare.ai with a comprehensive suite of laboratory tools and reagents, researchers can streamline their LB-100 investigations, optimize their research protocols, and accelerate the advancement of this important therapeutic target.