alectinib Search Results


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MedChemExpress alectinib
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Selleck Chemicals alectinib selleck chemicals s2762 alk
Alectinib Selleck Chemicals S2762 Alk, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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TargetMol alectinib t1936
Alectinib T1936, supplied by TargetMol, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MedChemExpress s2762 alectinib hydrochloride
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TargetMol alectinib hydrochloride
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BOC Sciences alectinib

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LKT Laboratories alk inhibitor
BiCAT analysis for cultured cancer cells. A, Representative image of <t>EML4‐ALK</t> primary cells. B, C, Partner molecules with CHL1 in EML4‐ALK primary cells were labeled with fluorescein‐arylazide (B) and fluorescein‐tyramide (C) reagent. Enzyme‐mediated activation of radical source (EMARS) products were, respectively, subjected to western blot analysis followed by staining using anti–fluorescein antibody. “CTxB” indicates the positive control sample using CTxB probe, “CHL1” the samples using CHL1 probe, and “(−)” the negative control samples (no probe). D, EMARS products labeled with fluorescein‐tyramide in LK2 cells. Protein expression level of CHL1 in LK2 and RERF cells (left column). EMARS products by CTxB and human CHL1 probes (right column). Abbreviations are the same as in (C). E, Human receptor tyrosine kinase (RTK) antibody array analysis of EMARS products from LK2 cells. EMARS samples were applied to Human RTK antibody array according to the manufacturer's instructions. “CHL1 probe (+)” indicates the sample using CHL1 probe, and “CHL1 probe (−)” the negative control samples (no probe). The proteins corresponding to positive RTK were indicated in the array data. F, Interaction between FGFR3 and <t>α2</t> <t>integrin</t> in HEK293 cells. HEK293 (mock) and CHL1 transfectant (hCHL1) cells were subjected to western blot analysis with anti–CHL1 antibody (left panel). The EMARS products by HRP‐conjugated anti CHL1 antibody from HEK293 and CHL1 transfectant cells were subjected to 10% SDS‐PAGE gel followed by direct fluorescein detection (middle panel). Immunoprecipitation experiment of fluorescein‐labeled α2 integrin using anti–fluorescein‐Sepharose (right panel). The immunoprecipitation samples and input lysate were subjected to 6% SDS‐PAGE gel followed by the western blot analysis with anti–α2 integrin antibody
Alk Inhibitor, supplied by LKT Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Biosynth Carbosynth alectinib hydrochloride
Figure 1. The inhibitory role of <t>Alectinib</t> on EML4-ALK-positive NSCLC.
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Selleck Chemicals alectinb

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Nagai Nori USA INC alectinib

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Genentech inc alectinib
Advances of ALK/ROS1-TKIs
Alectinib, supplied by Genentech inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Journal: iScience

Article Title: Overcoming MET-mediated resistance in oncogene-driven NSCLC

doi: 10.1016/j.isci.2023.107006

Figure Lengend Snippet:

Article Snippet: alectinib , BOC Sciences , NA.

Techniques: Recombinant, Synthesized, Hybridization, Software

BiCAT analysis for cultured cancer cells. A, Representative image of EML4‐ALK primary cells. B, C, Partner molecules with CHL1 in EML4‐ALK primary cells were labeled with fluorescein‐arylazide (B) and fluorescein‐tyramide (C) reagent. Enzyme‐mediated activation of radical source (EMARS) products were, respectively, subjected to western blot analysis followed by staining using anti–fluorescein antibody. “CTxB” indicates the positive control sample using CTxB probe, “CHL1” the samples using CHL1 probe, and “(−)” the negative control samples (no probe). D, EMARS products labeled with fluorescein‐tyramide in LK2 cells. Protein expression level of CHL1 in LK2 and RERF cells (left column). EMARS products by CTxB and human CHL1 probes (right column). Abbreviations are the same as in (C). E, Human receptor tyrosine kinase (RTK) antibody array analysis of EMARS products from LK2 cells. EMARS samples were applied to Human RTK antibody array according to the manufacturer's instructions. “CHL1 probe (+)” indicates the sample using CHL1 probe, and “CHL1 probe (−)” the negative control samples (no probe). The proteins corresponding to positive RTK were indicated in the array data. F, Interaction between FGFR3 and α2 integrin in HEK293 cells. HEK293 (mock) and CHL1 transfectant (hCHL1) cells were subjected to western blot analysis with anti–CHL1 antibody (left panel). The EMARS products by HRP‐conjugated anti CHL1 antibody from HEK293 and CHL1 transfectant cells were subjected to 10% SDS‐PAGE gel followed by direct fluorescein detection (middle panel). Immunoprecipitation experiment of fluorescein‐labeled α2 integrin using anti–fluorescein‐Sepharose (right panel). The immunoprecipitation samples and input lysate were subjected to 6% SDS‐PAGE gel followed by the western blot analysis with anti–α2 integrin antibody

Journal: Cancer Science

Article Title: Proximity proteomics identifies cancer cell membrane cis ‐molecular complex as a potential cancer target

doi: 10.1111/cas.14108

Figure Lengend Snippet: BiCAT analysis for cultured cancer cells. A, Representative image of EML4‐ALK primary cells. B, C, Partner molecules with CHL1 in EML4‐ALK primary cells were labeled with fluorescein‐arylazide (B) and fluorescein‐tyramide (C) reagent. Enzyme‐mediated activation of radical source (EMARS) products were, respectively, subjected to western blot analysis followed by staining using anti–fluorescein antibody. “CTxB” indicates the positive control sample using CTxB probe, “CHL1” the samples using CHL1 probe, and “(−)” the negative control samples (no probe). D, EMARS products labeled with fluorescein‐tyramide in LK2 cells. Protein expression level of CHL1 in LK2 and RERF cells (left column). EMARS products by CTxB and human CHL1 probes (right column). Abbreviations are the same as in (C). E, Human receptor tyrosine kinase (RTK) antibody array analysis of EMARS products from LK2 cells. EMARS samples were applied to Human RTK antibody array according to the manufacturer's instructions. “CHL1 probe (+)” indicates the sample using CHL1 probe, and “CHL1 probe (−)” the negative control samples (no probe). The proteins corresponding to positive RTK were indicated in the array data. F, Interaction between FGFR3 and α2 integrin in HEK293 cells. HEK293 (mock) and CHL1 transfectant (hCHL1) cells were subjected to western blot analysis with anti–CHL1 antibody (left panel). The EMARS products by HRP‐conjugated anti CHL1 antibody from HEK293 and CHL1 transfectant cells were subjected to 10% SDS‐PAGE gel followed by direct fluorescein detection (middle panel). Immunoprecipitation experiment of fluorescein‐labeled α2 integrin using anti–fluorescein‐Sepharose (right panel). The immunoprecipitation samples and input lysate were subjected to 6% SDS‐PAGE gel followed by the western blot analysis with anti–α2 integrin antibody

Article Snippet: After 72 hours, antibody and/or chemical inhibitors against CHL1, FGFR3 α2 integrin and EML4‐ALK were added to medium as follows: anti–mouse CHL1 antibody (AF2147; final concentration 2.5 μg/mL), anti–human CHL1 antibody (MAB2126; final concentration 2.5 μg/mL), FGFR inhibitor (PD173074; Cayman Chemical; final concentration 30 nmol/L), α2β1 integrin inhibitor (BTT3033; R&D systems; final concentration; 150 nmol/L) , and ALK inhibitor (CH5424802; LKT Laboratories; final concentration; 500 or 1000 nmol/L).

Techniques: Cell Culture, Labeling, Activation Assay, Western Blot, Staining, Positive Control, Negative Control, Expressing, Ab Array, Transfection, SDS Page, Immunoprecipitation

In vitro simulation of effective drug combination to inhibit cancer cell proliferation based on BiCAT information. A, The single and double administration under daily treatment protocol (n = 5). The administration timing is indicated by closed triangles. The cell numbers of the treated cells were measured on Day 2 and Day 4. B, The relative ratio (% of non–treated cells as control) of cell proliferation rates in LK2 cells and EML4‐ALK primary cells. The statistical analysis was performed using Tukey's test and Dunnett's multiple test. The results from Dunnett's test are presented in Figure 6; * P < 0.05; ** P < 0.005; ***P < 0.001. C, Double administration of molecular targeted reagents leads to changes in the expression of partner molecules. The samples of single and double administration under daily treatment conditions (3 d) in LK2 cells were subjected to phos‐tag SDS‐PAGE and then western blot analysis using CHL1, α2 integrin and FGFR3 antibodies. The CBB staining image indicates load control. The molecular weight markers were not shown in this figure because phos‐tag SDS‐PAGE cannot show the correct molecular weight of sample proteins. D, Western blot analysis of phosphorylated FGFR3 in single and double administration samples. The samples under daily treatment conditions (3 d) in LK2 cells were subjected to normal SDS‐PAGE gel and then western blot analysis using anti–FGFR3 and anti–phospho‐FGFR3 antibodies. The quantification of the phosphorylated bands detected in FGFR3 blots was performed using Image J software (ver. 1.51). The ratio of phosphorylation among the samples is indicated below the figure. E, Western blot analysis of phospho‐focal adhesion kinase (FAK) in single and double administration samples. The samples under daily treatment conditions (3 d) in LK2 cells were subjected to normal SDS‐PAGE and then western blot analysis using anti–FAK and anti–phospho‐FAK antibodies

Journal: Cancer Science

Article Title: Proximity proteomics identifies cancer cell membrane cis ‐molecular complex as a potential cancer target

doi: 10.1111/cas.14108

Figure Lengend Snippet: In vitro simulation of effective drug combination to inhibit cancer cell proliferation based on BiCAT information. A, The single and double administration under daily treatment protocol (n = 5). The administration timing is indicated by closed triangles. The cell numbers of the treated cells were measured on Day 2 and Day 4. B, The relative ratio (% of non–treated cells as control) of cell proliferation rates in LK2 cells and EML4‐ALK primary cells. The statistical analysis was performed using Tukey's test and Dunnett's multiple test. The results from Dunnett's test are presented in Figure 6; * P < 0.05; ** P < 0.005; ***P < 0.001. C, Double administration of molecular targeted reagents leads to changes in the expression of partner molecules. The samples of single and double administration under daily treatment conditions (3 d) in LK2 cells were subjected to phos‐tag SDS‐PAGE and then western blot analysis using CHL1, α2 integrin and FGFR3 antibodies. The CBB staining image indicates load control. The molecular weight markers were not shown in this figure because phos‐tag SDS‐PAGE cannot show the correct molecular weight of sample proteins. D, Western blot analysis of phosphorylated FGFR3 in single and double administration samples. The samples under daily treatment conditions (3 d) in LK2 cells were subjected to normal SDS‐PAGE gel and then western blot analysis using anti–FGFR3 and anti–phospho‐FGFR3 antibodies. The quantification of the phosphorylated bands detected in FGFR3 blots was performed using Image J software (ver. 1.51). The ratio of phosphorylation among the samples is indicated below the figure. E, Western blot analysis of phospho‐focal adhesion kinase (FAK) in single and double administration samples. The samples under daily treatment conditions (3 d) in LK2 cells were subjected to normal SDS‐PAGE and then western blot analysis using anti–FAK and anti–phospho‐FAK antibodies

Article Snippet: After 72 hours, antibody and/or chemical inhibitors against CHL1, FGFR3 α2 integrin and EML4‐ALK were added to medium as follows: anti–mouse CHL1 antibody (AF2147; final concentration 2.5 μg/mL), anti–human CHL1 antibody (MAB2126; final concentration 2.5 μg/mL), FGFR inhibitor (PD173074; Cayman Chemical; final concentration 30 nmol/L), α2β1 integrin inhibitor (BTT3033; R&D systems; final concentration; 150 nmol/L) , and ALK inhibitor (CH5424802; LKT Laboratories; final concentration; 500 or 1000 nmol/L).

Techniques: In Vitro, Control, Expressing, SDS Page, Western Blot, Staining, Molecular Weight, Software, Phospho-proteomics

Figure 1. The inhibitory role of Alectinib on EML4-ALK-positive NSCLC.

Journal: Pharmaceutics

Article Title: Alectinib-Loaded Chitosan–Alginate Nanoparticles: A Novel Synthesis Method with In Vitro and In Vivo Evaluations

doi: 10.3390/pharmaceutics17040492

Figure Lengend Snippet: Figure 1. The inhibitory role of Alectinib on EML4-ALK-positive NSCLC.

Article Snippet: Alectinib hydrochloride was obtained from (Biosynth Zurich, Switzerland, distributed by Cymit Química S.L., Barcelona, Spain) while dimethyl sulfoxide (DMSO) was sourced from EMSURE® in Grove Village, IL, USA.

Techniques:

Figure 3. The synthesis process of Alectinib-loaded chitosan–alginate nanoparticles.

Journal: Pharmaceutics

Article Title: Alectinib-Loaded Chitosan–Alginate Nanoparticles: A Novel Synthesis Method with In Vitro and In Vivo Evaluations

doi: 10.3390/pharmaceutics17040492

Figure Lengend Snippet: Figure 3. The synthesis process of Alectinib-loaded chitosan–alginate nanoparticles.

Article Snippet: Alectinib hydrochloride was obtained from (Biosynth Zurich, Switzerland, distributed by Cymit Química S.L., Barcelona, Spain) while dimethyl sulfoxide (DMSO) was sourced from EMSURE® in Grove Village, IL, USA.

Techniques:

Figure 5. The chromatogram of Alectinib 12.5 µg/mL solution in methanol and the chromatogram of the mobile phase.

Journal: Pharmaceutics

Article Title: Alectinib-Loaded Chitosan–Alginate Nanoparticles: A Novel Synthesis Method with In Vitro and In Vivo Evaluations

doi: 10.3390/pharmaceutics17040492

Figure Lengend Snippet: Figure 5. The chromatogram of Alectinib 12.5 µg/mL solution in methanol and the chromatogram of the mobile phase.

Article Snippet: Alectinib hydrochloride was obtained from (Biosynth Zurich, Switzerland, distributed by Cymit Química S.L., Barcelona, Spain) while dimethyl sulfoxide (DMSO) was sourced from EMSURE® in Grove Village, IL, USA.

Techniques:

Figure 7. The FTIR spectra of Alectinib, chitosan, alginate, and their mixture.

Journal: Pharmaceutics

Article Title: Alectinib-Loaded Chitosan–Alginate Nanoparticles: A Novel Synthesis Method with In Vitro and In Vivo Evaluations

doi: 10.3390/pharmaceutics17040492

Figure Lengend Snippet: Figure 7. The FTIR spectra of Alectinib, chitosan, alginate, and their mixture.

Article Snippet: Alectinib hydrochloride was obtained from (Biosynth Zurich, Switzerland, distributed by Cymit Química S.L., Barcelona, Spain) while dimethyl sulfoxide (DMSO) was sourced from EMSURE® in Grove Village, IL, USA.

Techniques:

Figure 8. DSC thermograms of pure Alectinib, chitosan, alginate, and ACANPs showing changes in thermal behavior, indicating drug encapsulation and transformation into the amorphous state.

Journal: Pharmaceutics

Article Title: Alectinib-Loaded Chitosan–Alginate Nanoparticles: A Novel Synthesis Method with In Vitro and In Vivo Evaluations

doi: 10.3390/pharmaceutics17040492

Figure Lengend Snippet: Figure 8. DSC thermograms of pure Alectinib, chitosan, alginate, and ACANPs showing changes in thermal behavior, indicating drug encapsulation and transformation into the amorphous state.

Article Snippet: Alectinib hydrochloride was obtained from (Biosynth Zurich, Switzerland, distributed by Cymit Química S.L., Barcelona, Spain) while dimethyl sulfoxide (DMSO) was sourced from EMSURE® in Grove Village, IL, USA.

Techniques: Encapsulation, Transformation Assay

Figure 11. (A) LC-MS/MS chromatogram for the blank sample with no peak of Alectinib. (B) Alectinib at 483,300 Da, height: 2.48 × 103 cps, RT: 0.504 min. (C) Rosuvastatin (internal standard) at 482,200 Da, height: 1.64 × 105 cps, RT: 0.750 min.

Journal: Pharmaceutics

Article Title: Alectinib-Loaded Chitosan–Alginate Nanoparticles: A Novel Synthesis Method with In Vitro and In Vivo Evaluations

doi: 10.3390/pharmaceutics17040492

Figure Lengend Snippet: Figure 11. (A) LC-MS/MS chromatogram for the blank sample with no peak of Alectinib. (B) Alectinib at 483,300 Da, height: 2.48 × 103 cps, RT: 0.504 min. (C) Rosuvastatin (internal standard) at 482,200 Da, height: 1.64 × 105 cps, RT: 0.750 min.

Article Snippet: Alectinib hydrochloride was obtained from (Biosynth Zurich, Switzerland, distributed by Cymit Química S.L., Barcelona, Spain) while dimethyl sulfoxide (DMSO) was sourced from EMSURE® in Grove Village, IL, USA.

Techniques: Liquid Chromatography with Mass Spectroscopy

Journal: iScience

Article Title: AXL and SHC1 confer crizotinib resistance in patient-derived xenograft model of ALK-driven lung cancer

doi: 10.1016/j.isci.2024.110846

Figure Lengend Snippet:

Article Snippet: Alectinb , Selleck Chemicals , Cat#S5232.

Techniques: Recombinant, Proliferation Assay, cDNA Synthesis, Multiplex Assay, Sequencing, Mass Spectrometry, DNA Sequencing

Advances of ALK/ROS1-TKIs

Journal: Journal of Hematology & Oncology

Article Title: Tyrosine kinase inhibitors for solid tumors in the past 20 years (2001–2020)

doi: 10.1186/s13045-020-00977-0

Figure Lengend Snippet: Advances of ALK/ROS1-TKIs

Article Snippet: Alectinib , Alecensa , Genentech Inc , ALK , Unresectable, advanced or recurrent ALK + NSCLC , 2014 §.

Techniques: