We provide robust and sensitive in vitro screening and characterization platforms for accelerating the discovery and screening of potential therapies for Lung Cancer. Our service offers comprehensive profiling of candidate compounds against relevant lung cancer targets, enabling rapid identification of promising therapeutic agents. Key targets and pathways include EGFR, ALK, KRAS mutations, and associated signaling cascades implicated in lung tumorigenesis and progression. We can assess compound effects on cell proliferation, apoptosis, receptor-ligand interactions, and other pathological processes central to lung cancer biology.
Our portfolio includes a diverse range of biochemical, cell-based, and biophysical assays tailored to evaluate the efficacy and mechanism of candidate compounds. These methods enable precise measurement of binding affinities, functional inhibition, and pathway modulation relevant to lung cancer.
AMP as substrate: Utilizes adenosine monophosphate as a substrate to assess enzyme activity or inhibition relevant to cancer metabolism and signaling.
ATP assay: Measures cellular ATP levels as an indicator of cell viability, cytotoxicity, and metabolic activity in response to drug candidates.
Chemiluminescent assay: Employs chemiluminescence to detect specific biomolecular interactions or enzymatic activities, providing sensitive readouts of drug efficacy.
Displacement of [3H]-ketanserin: Evaluates compound binding to specific receptor sites by measuring the displacement of radiolabeled ligands, informative for receptor-targeted therapies.
Flow cytometry assay: Analyzes cell populations for markers of proliferation, apoptosis, or surface receptor expression, allowing for multiparametric assessment of drug effects.
Surface plasmon resonance assay: Provides real-time analysis of biomolecular interactions, enabling precise determination of binding kinetics and affinities between drug candidates and targets.
We measure key pharmacological parameters including inhibitory concentration (IC-50), binding affinity (Kd), and ligand-receptor interaction strength (pKi). These parameters are critical for characterizing compound potency, selectivity, and therapeutic potential in lung cancer drug development.
IC-50: The concentration of a compound required to inhibit a biological process or target by 50%, serving as a primary indicator of drug potency.
Kd: The equilibrium dissociation constant that quantifies the binding affinity between a ligand and its target; lower Kd values indicate stronger interactions.
pKi: The negative logarithm of the inhibition constant (Ki), reflecting the strength of inhibitor binding to its target; higher pKi values correspond to higher binding affinity.
5'-Nucleotidase Ecto (CD73) promotes immunosuppression and tumor progression in lung cancer by generating adenosine from AMP. Testing its activity is crucial for evaluating drug efficacy and immune modulation. Our service uses flow cytometry, surface plasmon resonance, and chemiluminescent assays with AMP as a substrate to quantify enzyme activity and drug binding. Key parameters measured include Kd (binding affinity) and IC-50 (inhibitory potency), essential for drug development and optimization.
| Pharmacological Activity | Material | Method | Parameter |
|---|---|---|---|
| 5'-Nucleotidase affinity | CHO-K1 Chinese hamster ovary cells transfected with human enzyme | Flow cytometry assay | IC-50 |
| 5'-Nucleotidase affinity | Recombinant human enzyme | Surface plasmon resonance assay | Kd |
| 5'-Nucleotidase, inhibition | CHO Chinese hamster ovary cells transfected with human enzyme | AMP as substrate | IC-50 |
| 5'-Nucleotidase, inhibition | CHO-K1 Chinese hamster ovary cells transfected with human enzyme | Chemiluminescent assay | IC-50 |
| 5'-Nucleotidase, inhibition | MDAMB231 human breast adenocarcinoma cells | AMP as substrate | IC-50 |
| 5'-Nucleotidase, inhibition | Recombinant human enzyme | AMP as substrate | IC-50 |
| 5'-Nucleotidase, inhibition | Recombinant human enzyme | Chemiluminescent assay | IC-50 |
The 5-Hydroxytryptamine Receptor 2A (5-HT2A) is implicated in lung cancer progression and drug response. Testing its binding characteristics is essential for identifying and optimizing targeted therapies. Our service employs [3H]-ketanserin displacement assays to evaluate ligand-receptor interactions, providing precise IC₅₀ and pKi values. These parameters enable effective screening of novel compounds and support rational drug development for lung cancer treatment.
| Pharmacological Activity | Material | Method | Parameter |
|---|---|---|---|
| G-Protein (receptor-linked) activation, inhibition | Cells transfected with 5-HT2A receptor | IC-50 | |
| Serotonin 5-HT2A receptor affinity | CHO Chinese hamster ovary cells transfected with human receptor | Displacement of [3H]-ketanserin | pKi |
A-Raf Proto-Oncogene, Serine/Threonine Kinase regulates crucial signaling pathways in lung cancer progression. Testing its activity is vital for identifying potential therapeutic inhibitors. Our service employs ATP assays to evaluate kinase inhibition, providing precise IC-50 values for drug candidates. This enables efficient screening and optimization of compounds targeting A-Raf, accelerating lung cancer drug development with robust, actionable data.
| Pharmacological Activity | Material | Method | Parameter |
|---|---|---|---|
| Serine/threonine protein kinase (A-Raf) (G377R-mutated), inhibition | Recombinant enzyme | ATP assay | IC-50 |
| Serine/threonine protein kinase (A-Raf) (P462L-mutated), inhibition | Recombinant enzyme | ATP assay | IC-50 |
| Serine/threonine protein kinase (A-Raf) (del 347_348 (G387D)-mutated), inhibition | Recombinant enzyme | ATP assay | IC-50 |
| Serine/threonine protein kinase (A-Raf) (del 347_348-mutated), inhibition | Recombinant enzyme | ATP assay | IC-50 |
| Serine/threonine protein kinase (A-Raf), inhibition | Recombinant enzyme | ATP assay | IC-50 |
Abl Proto-Oncogene 1, Non-Receptor Tyrosine Kinase (ABL1) is implicated in lung cancer progression by promoting cell proliferation and survival. Testing its activity is crucial for identifying targeted therapies and evaluating drug efficacy. Our service employs chemiluminescent and ATP assays to accurately measure ABL1 kinase activity. The primary parameter assessed is IC-50, enabling precise determination of compound potency for lung cancer drug development.
| Pharmacological Activity | Material | Method | Parameter |
|---|---|---|---|
| Protein-tyrosine kinase (Abl) (T315I-mutated), inhibition | Chemiluminescent assay | IC-50 | |
| Protein-tyrosine kinase (Bcr-Abl) (H396P-mutated), inhibition | Recombinant human enzyme | ATP assay | IC-50 |
| Protein-tyrosine kinase (Bcr-Abl) (M351T-mutated), inhibition | Recombinant human enzyme | ATP assay | IC-50 |
| Protein-tyrosine kinase (Bcr-Abl) (Q252H-mutated), inhibition | Recombinant human enzyme | ATP assay | IC-50 |
| Protein-tyrosine kinase (Bcr-Abl) (T315I-mutated), inhibition | Recombinant human enzyme | ATP assay | IC-50 |
| Protein-tyrosine kinase (Bcr-Abl), inhibition | Recombinant human enzyme | ATP assay | IC-50 |
| Protein-tyrosine kinase (Bcr-Abl), inhibition | Chemiluminescent assay | IC-50 |
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