Contact Us

The choice depends on whether you are studying TNFR2-specific signaling — distinct from TNFR1 — or its emerging role in Treg biology and tumor immunity. The Knockout line is appropriate for asking whether TNFR2 is required for non-classical TNF signaling, including TRAF2-mediated NF-κB activation and anti-apoptotic signaling. Overexpression is useful for testing whether elevated TNFR2 is sufficient to enhance these pathways. For TNF biology research, the EDITGENE Knockout in HAP1 is particularly informative when combined with the parallel TNFR1 knockout — comparison of single and combined knockouts dissects receptor-specific TNF functions, since TNF binds both receptors with different affinities and signaling consequences. Rescue with wild-type or signaling domain-deleted TNFR2 is the standard approach for assigning observed phenotypes to specific TNFR2 signaling outputs.

Yes. TNFR2 rescue experiments require attention to receptor topology and signaling specificity: • Construct design: use a codon-modified TNFRSF1B sequence with a cytoplasmic C-terminal tag (FLAG, HA). TNFR2 is a type I membrane protein — the extracellular cysteine-rich domains and the cytoplasmic tail must both be preserved. • Surface expression validation: confirm exogenous TNFR2 surface localization by flow cytometry before downstream signaling assays. • Signaling domain mutant rescue: TRAF2-binding-deficient mutations separate ligand binding from intracellular signaling functions. • Functional readout: rescue should restore TRAF2-mediated NF-κB activation and TNFR2-specific gene expression patterns. HAP1-specific considerations: • Diploidization: HAP1 cells gradually diploidize during extended culture — confirm ploidy by flow cytometry at the time of phenotypic assay. • Integration site sensitivity: position effects on transgene expression are more pronounced in near-haploid backgrounds; generating multiple independent rescue clones is strongly recommended. • Transduction efficiency: HAP1 transduces with lentivirus at moderate efficiency — increase MOI compared to standard immortalized lines.

The choice depends on whether you are studying TAOK2's role in MAP kinase signaling, autism-spectrum-related neuronal biology, or DNA damage response. The Knockout line is appropriate for asking whether TAOK2 is required for these pathways — TAOK2 has been implicated in 16p11.2 deletion-associated neurodevelopmental phenotypes. Overexpression is useful for testing whether elevated TAOK2 activity drives specific signaling outputs or for studying 16p11.2 duplication-related phenotypes. Important consideration: TAOK1 and TAOK3 share substantial overlap with TAOK2 in MAPK signaling. The EDITGENE Knockout line is most informative when paralog status is assessed; combined analysis with the parallel TAOK3 knockout enables family-specific dissection. Rescue with wild-type, kinase-dead, or autism-associated variant TAOK2 enables mechanistic and disease-modeling studies.

The choice depends on whether you are studying TEC kinase's role in immune cell signaling or its emerging functions outside hematopoietic contexts. Important consideration: TEC kinase is normally expressed in T cells, mast cells, and other hematopoietic lineages — HAP1 (myeloid origin) has detectable but modest TEC expression. The Knockout line is appropriate for asking whether TEC contributes to signaling in this hematopoietic-related background, but physiological TEC functions are best studied in T cell or mast cell systems. Overexpression in HAP1 may be more informative for biochemical studies of TEC kinase activity, substrate phosphorylation, and inhibitor specificity testing. The EDITGENE Knockout line is useful as a clean genetic background for distinguishing TEC from its family paralogs (BTK, ITK, BMX, TXK), and as a specificity control for TEC kinase inhibitors. Rescue with wild-type or kinase-dead TEC is the standard control.

Yes. TEC rescue experiments require attention to its multi-domain architecture: • Construct design: use a codon-modified TEC sequence with a C-terminal tag (FLAG, HA). TEC contains PH, SH3, SH2, and kinase domains — all must be preserved. • Kinase-dead rescue: the K398R mutation in the active site abolishes catalytic activity and is the standard specificity control. • Domain-specific mutants: PH-domain mutations (PI(3,4,5)P3-binding-deficient) and SH3/SH2 domain mutations enable dissection of membrane recruitment versus substrate engagement. • Inhibitor selectivity controls: TEC family inhibitors often show cross-reactivity — rescue with wild-type or specific inhibitor-resistant TEC variants is valuable for assessing on-target activity. HAP1-specific considerations: • Diploidization: HAP1 cells gradually diploidize during extended culture — confirm ploidy by flow cytometry at the time of phenotypic assay. • Integration site sensitivity: position effects on transgene expression are more pronounced in near-haploid backgrounds; generating multiple independent rescue clones is strongly recommended. • Transduction efficiency: HAP1 transduces with lentivirus at moderate efficiency — increase MOI compared to standard immortalized lines.

The choice depends on whether you are studying TNFR1-specific signaling — distinct from TNFR2 — or its role in inflammatory and cell death pathways. The Knockout line is appropriate for asking whether TNFR1 is required for classical TNF signaling, including death-domain-mediated apoptosis/necroptosis and NF-κB activation. Overexpression is useful for studying TNFR1-driven gain-of-function or modeling TRAPS (TNFR1-associated periodic syndromes) mutations. For TNF biology research, the EDITGENE Knockout in HAP1 is the standard tool — TNFR1 is the principal mediator of TNF cytotoxicity and inflammatory signaling. Combined analysis with the TNFR2 knockout (also available) enables comprehensive receptor-specific dissection. Rescue with wild-type, death-domain-deleted, or TRAPS-associated mutant TNFR1 enables disease modeling and signaling pathway dissection.

Yes. TNFR1 rescue experiments require attention to death-domain function and trimerization: • Construct design: use a codon-modified TNFRSF1A sequence with a cytoplasmic C-terminal tag (FLAG, HA). TNFR1 is a type I membrane protein with an essential intracellular death domain. • Death-domain-deleted rescue: deletion of the death domain separates ligand-binding/recruitment from apoptosis-inducing functions. • TRAPS-associated mutant rescue: introduction of TRAPS variants enables modeling of TNFR1-associated periodic syndromes. • Functional readout: rescue should restore TNF-α-induced apoptosis (caspase-8/3 cleavage) and NF-κB activation (p65 phosphorylation, IκBα degradation). HAP1-specific considerations: • Diploidization: HAP1 cells gradually diploidize during extended culture — confirm ploidy by flow cytometry at the time of phenotypic assay. • Integration site sensitivity: position effects on transgene expression are more pronounced in near-haploid backgrounds; generating multiple independent rescue clones is strongly recommended. • Transduction efficiency: HAP1 transduces with lentivirus at moderate efficiency — increase MOI compared to standard immortalized lines.

The choice depends on whether you are studying TAOK3's role in MAP kinase signaling, stress response activation, or B cell receptor signaling (in physiological contexts). The Knockout line is appropriate for asking whether TAOK3 is required for MAP3K-mediated activation of stress kinase pathways. Overexpression is useful for testing whether elevated TAOK3 is sufficient to drive p38/JNK activation or for biochemical studies of substrate phosphorylation. Important consideration: TAOK1, TAOK2, and TAOK3 share substantial functional overlap in MAPK signaling. Single TAOK3 knockout in HAP1 may show mild phenotypes if its paralogs compensate. Combined analysis with the parallel TAOK2 knockout (also available from EDITGENE) enables paralog-specific dissection. Rescue with wild-type or kinase-dead TAOK3 is the standard specificity control.

Yes. TAOK3 rescue experiments require attention to kinase activity and family paralog considerations: • Construct design: use a codon-modified TAOK3 sequence with a small C-terminal tag (FLAG, HA). The N-terminal kinase domain must be preserved. • Kinase-dead rescue: an active site mutation (typically in the catalytic loop) abolishes kinase activity and is the standard specificity control. • Paralog rescue panel: rescue with TAOK3 in TAOK2 single knockouts (or vice versa) enables family-specific functional dissection. • Functional readout: rescue should restore stress-induced p38/JNK activation patterns. HAP1-specific considerations: • Diploidization: HAP1 cells gradually diploidize during extended culture — confirm ploidy by flow cytometry at the time of phenotypic assay. • Integration site sensitivity: position effects on transgene expression are more pronounced in near-haploid backgrounds; generating multiple independent rescue clones is strongly recommended. • Transduction efficiency: HAP1 transduces with lentivirus at moderate efficiency — increase MOI compared to standard immortalized lines.

The choice depends on whether you are studying TNIK's role in Wnt/β-catenin signaling, its scaffolding functions, or its emerging status as a fibrosis and cancer drug target. The Knockout line is appropriate for asking whether TNIK is required for these processes — TNIK functions as both a kinase and a scaffold for Wnt pathway components. Overexpression is useful for studying TNIK gain-of-function or for distinguishing kinase from scaffolding activities through kinase-dead variants. For TNIK research, the EDITGENE Knockout line in HAP1 is particularly valuable because TNIK inhibitors are in clinical development for cancer and IPF — this knockout provides a critical genetic specificity control for testing on-target activity of those compounds. Rescue with wild-type or kinase-dead TNIK is essential for distinguishing catalytic from scaffolding contributions.

Yes. TNIK rescue experiments require attention to its dual kinase-scaffold nature: • Construct design: use a codon-modified TNIK sequence with a small C-terminal tag (FLAG, HA). TNIK is large (~1,360 amino acids); both kinase and protein interaction domains must be preserved. • Kinase-dead rescue: the K54A mutation in the ATP-binding lysine abolishes catalytic activity and is the standard control for separating kinase from scaffolding functions. • Scaffolding-deficient rescue: C-terminal truncation or mutation of protein interaction motifs separates substrate phosphorylation from complex assembly functions. • TNIK inhibitor controls: rescue with wild-type and kinase-dead TNIK enables direct assessment of whether TNIK inhibitors act through catalytic inhibition or additional off-target mechanisms. HAP1-specific considerations: • Diploidization: HAP1 cells gradually diploidize during extended culture — confirm ploidy by flow cytometry at the time of phenotypic assay. • Integration site sensitivity: position effects on transgene expression are more pronounced in near-haploid backgrounds; generating multiple independent rescue clones is strongly recommended. • Transduction efficiency: HAP1 transduces with lentivirus at moderate efficiency — increase MOI compared to standard immortalized lines.

The choice depends on whether you are studying TMEM65's role in mitochondrial cristae organization and respiratory chain maintenance, or modeling encephalomyopathy phenotypes. The Knockout line is appropriate for asking whether TMEM65 is required for mitochondrial function in colorectal cancer cells. Overexpression is useful for testing sufficiency or for rescue with disease-associated TMEM65 variants. For TMEM65 research, the EDITGENE Knockout in HCT116-LUC offers a unique advantage: the luciferase reporter enables in vivo bioluminescence imaging for xenograft studies, allowing researchers to assess how TMEM65 loss affects tumor growth and metabolism in animal models. Combined with mitochondrial function readouts (Seahorse, membrane potential), this provides a comprehensive in vitro/in vivo platform. Rescue with wild-type or disease-mutant TMEM65 enables structure-function and disease-modeling studies.

Yes. TMEM65 rescue experiments require attention to mitochondrial inner membrane targeting: • Construct design: use a codon-modified TMEM65 sequence with a small C-terminal tag (FLAG, HA). TMEM65 contains an N-terminal mitochondrial targeting sequence — N-terminal tags must not disrupt mitochondrial import. • Localization validation: confirm mitochondrial localization of exogenous TMEM65 by immunofluorescence co-staining with TOM20 or by mitochondrial fractionation before functional assays. • Disease mutation rescue: TMEM65 mutations associated with mitochondrial encephalomyopathy can be introduced for genotype-function studies. • Functional readout: rescue should restore mitochondrial membrane potential (TMRM), respiratory capacity (Seahorse), and cristae morphology (electron microscopy). HCT116-LUC transduces efficiently with lentivirus; the luciferase reporter is maintained through standard rescue line generation, preserving in vivo imaging capability.

The choice depends on whether you are studying TESK1's role in actin cytoskeleton regulation through cofilin phosphorylation, or its emerging functions in integrin signaling and immune regulation. The Knockout line is appropriate for asking whether TESK1 is required for cofilin-1 Ser3 phosphorylation in contexts where its paralog LIMK1/LIMK2 may not fully compensate. Overexpression is useful for testing whether elevated TESK1 activity is sufficient to drive cofilin phosphorylation and actin filament stabilization. For TESK1 research, the EDITGENE Knockout line in HAP1 provides a clean genetic background, though LIMK paralog compensation should be considered when interpreting phenotypes — single TESK1 knockout often shows mild cytoskeletal effects because LIMK1/LIMK2 catalyze the same cofilin phosphorylation. Rescue with wild-type or kinase-dead TESK1 is the standard control for distinguishing catalytic activity from scaffolding contributions.

Yes. TESK1 rescue experiments require attention to kinase activity and cofilin engagement: • Construct design: use a codon-modified TESK1 sequence with a C-terminal tag (FLAG, HA). TESK1's N-terminal kinase domain and C-terminal proline-rich region should both be preserved. • Kinase-dead rescue: the K53A mutation in the ATP-binding lysine abolishes catalytic activity and is the standard control for distinguishing kinase from non-catalytic functions. • LIMK paralog considerations: rescue interpretation should account for LIMK1/LIMK2 expression in HAP1 — these paralogs phosphorylate the same cofilin Ser3 site. • Functional readout: rescue should restore phospho-cofilin (Ser3) levels and downstream actin cytoskeleton phenotypes. HAP1-specific considerations: • Diploidization: HAP1 cells gradually diploidize during extended culture — confirm ploidy by flow cytometry at the time of phenotypic assay. • Integration site sensitivity: position effects on transgene expression are more pronounced in near-haploid backgrounds; generating multiple independent rescue clones is strongly recommended. • Transduction efficiency: HAP1 transduces with lentivirus at moderate efficiency — increase MOI compared to standard immortalized lines.