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Yes. S100A9 rescue experiments require attention to heterodimer biology: • Construct design: use a codon-modified S100A9 sequence with a small C-terminal tag (FLAG, HA). S100A9 is small (~114 amino acids) with two EF-hand calcium-binding domains — preserve N-terminal sequence that mediates S100A8 partnership. • Calcium-binding-deficient rescue: EF-hand mutations (canonical E to Q substitutions in the calcium-coordinating residues) abolish calcium binding and downstream conformational changes, serving as the standard specificity control. • S100A8 partnership: S100A9 functions primarily as the S100A8/A9 heterodimer — rescue interpretation should account for S100A8 expression in A-549. • Functional readout: rescue should restore calprotectin-dependent activities including TLR4/RAGE binding, MMP9 secretion modulation, and inflammatory signaling. A-549 transduces efficiently with lentivirus and supports stable rescue line generation.

Primary applications: • Calprotectin biology: S100A8/A9 heterodimer formation and stability analysis given functional dependence on the heterodimer. • Lung cancer phenotype: proliferation, migration, invasion, and EMT marker analysis in A-549 to assess S100A9's contribution to lung cancer biology. • Inflammatory signaling: NF-κB activation, cytokine production, and TLR4/RAGE signaling in response to inflammatory stimuli given S100A9's DAMP activity. • S100A9 inhibitor specificity: critical genetic control for paquinimod, tasquinimod, and other S100A8/A9-targeting compounds in cancer and autoimmune disease development. EDITGENE recommends this model for researchers investigating S100A9/calprotectin biology, lung cancer inflammation, and S100A8/A9-targeted therapeutic development.

The choice depends on whether you are studying S100A9 (MRP14, calgranulin B)'s role as a calcium-binding damage-associated molecular pattern (DAMP) or its functions as part of the S100A8/A9 calprotectin heterodimer in inflammation and cancer biology. The Knockout line is the standard tool for asking whether S100A9 is required for these processes — S100A9 is normally expressed by myeloid cells but is upregulated in many epithelial cancers including lung cancer (relevant to A-549), where it contributes to tumor progression and inflammation. Overexpression is useful for studying S100A9 in inflammation models or for testing its role in chemoattraction and innate immunity. For inflammation and cancer research, the EDITGENE S100A9 Knockout in A-549 is highly relevant — A-549 is a lung adenocarcinoma cell line, and S100A9 has been implicated in lung cancer progression, neutrophil extracellular trap formation, and chronic inflammation contexts. S100A8 (heterodimer partner) expression analysis is essential given that calprotectin functions primarily as the S100A8/A9 heterodimer. Rescue with wild-type or calcium-binding-deficient S100A9 enables structure-function studies. S100A9 inhibitors (paquinimod, tasquinimod) specificity testing benefits from this knockout.

Yes. CTH rescue experiments are well-established for transsulfuration research: • Construct design: use a codon-modified CTH sequence with a small C-terminal tag (FLAG, HA). CTH has the canonical PLP (pyridoxal 5'-phosphate)-dependent enzyme architecture — preserve all elements. • Catalytically-dead rescue: PLP-binding lysine mutations abolish γ-lyase activity and serve as the standard specificity control. • Functional readout: rescue should restore cysteine production from cystathionine and H₂S generation activity. A-549 transduces efficiently with lentivirus and supports stable rescue line generation.

Primary applications: • Transsulfuration biology: cysteine, glutathione (GSH) levels and homocysteine accumulation analysis in CTH-null cells. • H₂S production: cellular H₂S quantification by fluorescent probes (SF-7AM, AzMC) given CTH's role as one of three H₂S-generating enzymes. • Ferroptosis sensitivity: GPX4 activity and lipid peroxidation analysis given CTH's contribution to cysteine availability for GSH-GPX4 axis. • Lung cancer biology: NSCLC proliferation and chemotherapy sensitivity in A-549 context. EDITGENE recommends this lung cancer model for researchers investigating transsulfuration biology, H₂S signaling, ferroptosis defense, and CTH-targeted approaches.

The choice depends on whether you are studying CTH (cystathionine γ-lyase, CSE)'s role in transsulfuration and H₂S biosynthesis or modeling its functions in lung cancer and cysteine metabolism. The Knockout line is the standard tool for asking whether CTH is required for these processes — CTH catalyzes the second step of transsulfuration (cystathionine → cysteine + α-ketobutyrate + NH₃), generating cysteine from methionine-derived homocysteine; CTH is also one of three enzymes (with CBS and 3-MST) that generates H₂S, an endogenous gaseous signaling molecule with cardiovascular and anti-inflammatory effects. Overexpression is useful for studying CTH gain-of-function effects. For lung cancer and metabolic research, the EDITGENE CTH Knockout in A-549 is highly relevant — A-549 is an NSCLC cell line, and CTH-derived cysteine/H₂S has been implicated in NSCLC biology including glutathione synthesis and redox balance. Rescue with wild-type or catalytically-dead CTH enables structure-function studies. CTH biallelic loss causes cystathioninuria (autosomal recessive metabolic disorder). The knockout is valuable for studying transsulfuration biology, H₂S signaling, ferroptosis (cysteine availability for GSH synthesis), and emerging CTH-targeted approaches.

The kit employs advanced biomolecular transfection technology, offering significant advantages over traditional methods. Unlike chemical transfection, which may be cytotoxic, or electroporation, which can subject cells to physical stress, this approach ensures minimal damage while maintaining high efficiency.

This kit has been validated across multiple cell lines. The RNP complex enters cells and begins gene editing within 4 hours post-transfection. Cas9 protein is degraded within 24–48 hours, allowing efficient and transient expression-driven editing without the need for antibiotic or fluorescent selection.

While suspension cells are generally more difficult to transfect, this kit performs exceptionally well in both adherent and suspension cell types. For example, in Jurkat cells, editing efficiency can reach up to 97% within 48 hours post-transfection, demonstrating the kit’s outstanding performance and suitability for demanding suspension cell applications.

The product has been validated in multiple cell types. The RNP system enters cells and begins functioning within 4 hours post-transfection, and the Cas9 protein is degraded within 24-48 hours. This transient, high-efficiency expression enables gene editing without the need for continuous selection.

If gene knockout fails when using this kit, EDITGENE will not charge for the kit. Additionally, the fee you paid for the kit can be directly applied toward EDITGENE’s gene knockout service, ensuring that your gene editing experiments proceed without concerns.

The product utilizes advanced biomolecular transfection technology. Compared with the toxicity of traditional chemical transfection methods and the physical stress of electroporation, it shows significant advantages in preserving cell viability.

Transfecting suspension cells is generally more challenging. However, due to its superior performance, this product works efficiently not only in adherent cells but also in suspension cells. For example, in Jurkat cells, 48 hours post-transfection, editing efficiency can reach up to 97%, demonstrating the product’s high efficiency in suspension cell transfection and meeting demanding requirements.

Yes. FcRn rescue experiments require attention to heterodimer formation and pH-sensing: • Construct design: use a codon-modified FcRn (FCGRT) sequence with a small intracellular C-terminal tag (FLAG, HA). FcRn (FCGRT) heavy chain associates non-covalently with β2-microglobulin (B2M) for surface expression — both subunits required. • pH-binding-deficient rescue: H310A/H433A and other histidine residue mutations abolish pH-dependent IgG binding and serve as the standard specificity control. • B2M partnership: rescue interpretation considers B2M expression — both FCGRT heavy chain and B2M are required for surface FcRn. • Functional readout: rescue should restore pH 6.0 IgG binding and pH 7.4 IgG release, and IgG transcytosis activity. ST-specific considerations: • ST is a porcine testicular cell line widely used for swine virus research (transmissible gastroenteritis virus TGEV, porcine epidemic diarrhea virus PEDV) and porcine-specific receptor biology. • Lentiviral transduction efficiency in ST cells may require optimization; the porcine species background must be considered for ortholog and antibody cross-reactivity. • Cell line authentication is recommended.

The choice depends on whether you are studying FcRn (neonatal Fc receptor)'s role in IgG and albumin homeostasis or modeling porcine IgG biology and transcytosis. The Knockout line is the standard tool for asking whether FcRn is required for these processes — FcRn is a non-classical MHC class I-like receptor expressed on epithelial cells, endothelial cells, and antigen-presenting cells; FcRn binds IgG at acidic pH (early endosome) and releases at neutral pH (cell surface), enabling IgG transcytosis (gut absorption in neonates, placental transfer) and IgG recycling (extending IgG serum half-life to ~3 weeks). Overexpression is useful for studying FcRn in heterologous expression contexts. For porcine immunology and transcytosis research, the EDITGENE FcRn Knockout in ST is uniquely valuable — ST is a porcine testicular cell line, and porcine FcRn has specific applications in agricultural immunology and xenotransplantation research. Rescue with wild-type or pH-binding-deficient (H310A/H433A) FcRn enables structure-function studies. The knockout is valuable for studying IgG pharmacokinetics, antibody half-life extension strategies (YTE, LS, AAA mutations enhance FcRn binding), and FcRn antagonists (efgartigimod, FDA-approved for myasthenia gravis; rozanolixizumab; nipocalimab — for autoantibody-mediated diseases).