Contact Us

Yes. CDK4 rescue experiments are well-established for breast cancer drug research: • Construct design: use a codon-modified CDK4 sequence with a small C-terminal tag (FLAG, HA). CDK4 has the canonical CDK architecture — preserve all elements. • Kinase-dead rescue: K35R mutation in the ATP-binding lysine abolishes catalytic activity. • CDK4/6 inhibitor-resistant rescue: gatekeeper mutations can confer palbociclib/ribociclib/abemaciclib resistance for on-target validation. • Functional readout: rescue should restore Cyclin D-CDK4 kinase activity and phospho-RB1. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying CDK6's role as a G1/S phase kinase or modeling CDK4/6 inhibitor pharmacology for breast cancer therapy. The Knockout line is the standard tool for asking whether CDK6 is required for these processes — CDK6 partners with D-type cyclins (CCND1, CCND2, CCND3) to phosphorylate RB1 at G1/S transition, releasing E2F transcription factors for S-phase gene expression; CDK6 has substantial functional overlap with CDK4 but also distinct functions in hematopoietic differentiation, glucose metabolism, and AML. Overexpression is useful for studying CDK6 gain-of-function effects. Important consideration: CDK4 and CDK6 share substantial substrate scope — single CDK6 knockout may show modest phenotypes if CDK4 compensates. This product complements the parallel CDK4 Knockout in HEK293 (also available) for paralog-specific dissection. Rescue with wild-type or kinase-dead CDK6 is the standard specificity control. The knockout is a critical specificity tool for ⭐⭐⭐ palbociclib (Ibrance, FDA-approved 2015 for HR+/HER2− metastatic breast cancer), ribociclib (Kisqali), abemaciclib (Verzenio) — three FDA-approved CDK4/6 inhibitors that have transformed HR+ breast cancer treatment — and emerging CDK6-selective inhibitors and CDK6 degraders.

Yes. CDK6 rescue experiments are well-established for breast cancer drug research: • Construct design: use a codon-modified CDK6 sequence with a small C-terminal tag (FLAG, HA). CDK6 has the canonical CDK architecture (PSTAIRE motif in helix αC, T-loop with T177 activation phospho-site) — preserve all elements. • Kinase-dead rescue: K43R mutation in the ATP-binding lysine abolishes catalytic activity. • CDK4/6 inhibitor-resistant rescue: T-loop or gatekeeper residue mutations can confer palbociclib/ribociclib/abemaciclib resistance for on-target validation studies. • Functional readout: rescue should restore Cyclin D-CDK6 kinase activity and phospho-RB1 (S780, S795). HEK293 transduces efficiently with lentivirus and supports stable rescue line generation for systematic CDK4/6 inhibitor research.

The choice depends on whether you are studying CRBN (cereblon) in a complementary high-transfection-efficiency biochemistry platform — CRBN is the substrate receptor of the CRL4^CRBN E3 ubiquitin ligase and the molecular target of thalidomide, lenalidomide, pomalidomide, and the entire IMiD class and CRBN-recruiting PROTAC field. The Knockout line is the standard tool for asking whether CRBN is required for IMiD/molecular glue/PROTAC degrader activity — CRBN was identified as the thalidomide target and is the foundational molecular glue degrader receptor. Overexpression is useful for studying CRBN in heterologous expression contexts. For systematic CRBN biochemistry, the EDITGENE CRBN Knockout in HEK293 is a workhorse mechanistic platform — HEK293 supports systematic structure-function studies and high-throughput rescue mutant screening. This product complements the parallel CRBN Knockout in HeLa (also available); HEK293 is preferred for biochemistry and structure-function studies, HeLa for imaging-based and chemotherapy resistance studies. Rescue with wild-type or thalidomide-binding-pocket mutants (Y355A, W380A, W386A, W400A) enables systematic IMiD/molecular glue/PROTAC specificity testing. The knockout is a critical specificity tool for the entire CRBN-targeting therapeutic field including thalidomide, lenalidomide (Revlimid), pomalidomide (Pomalyst), iberdomide, mezigdomide, GSPT1 degraders (CC-90009), and CRBN-recruiting PROTACs (ARV-110, ARV-471, KT-474, NX-2127, DT2216).

Yes, and rescue experiments are uniquely powerful for IMiD/molecular glue/PROTAC research: • Construct design: use a codon-modified CRBN sequence with a small C-terminal tag (FLAG, HA). CRBN has N-terminal Lon protease-like domain, helical-bundle domain, and C-terminal thalidomide-binding domain (TBD) with the critical tri-tryptophan/Y pocket — preserve all elements. • Thalidomide-binding-pocket mutant rescue: ⭐⭐ Y355A, W380A, W386A, W400A mutations abolish IMiD binding — gold-standard specificity control for the entire CRBN-targeted therapeutic field. • IMiD resistance mutation rescue: clinical IMiD-resistant patient CRBN mutations enable resistance mechanism studies. • DDB1-binding-deficient rescue: N-terminal CRBN mutations disrupt CRL4 complex assembly. • Functional readout: rescue should restore IKZF1, IKZF3, CK1α, GSPT1 degradation upon IMiD/molecular glue treatment; thalidomide-binding-pocket mutants should be insensitive to all CRBN-recruiting compounds. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation for systematic CRBN mutant screening.

The choice depends on whether you are studying CASP3's role as the principal executioner caspase or modeling apoptosis and chemotherapy-induced pyroptosis in lung cancer. The Knockout line is the standard tool for asking whether CASP3 is required for these processes — CASP3 is the principal executioner caspase that cleaves >200 substrates (PARP1, ICAD/DFF45, ROCK1, lamins, GSDME) to execute apoptosis; CASP3 also cleaves GSDME at D270 to drive chemotherapy-induced pyroptosis (the apoptosis-to-pyroptosis switch in GSDME-expressing cells). Overexpression is useful for studying CASP3 gain-of-function effects. For lung cancer chemotherapy research, the EDITGENE CASP3 Knockout in A-549 is highly relevant — A-549 is an NSCLC cell line, and CASP3 is critical for chemotherapy-induced apoptosis in NSCLC. Rescue with wild-type or catalytically-dead (C163A) CASP3 is the standard specificity control. The knockout is paired with parallel GSDME Knockout in SK-OV-3 (also available) for studying chemotherapy-induced apoptosis-to-pyroptosis switching. The knockout is valuable for studying executioner caspase biology, chemotherapy-induced cell death mechanisms (cisplatin, paclitaxel), and immunogenic cell death pathways.

Yes. CASP3 rescue experiments are well-established for apoptosis research: • Construct design: use a codon-modified CASP3 sequence with a small C-terminal tag (FLAG, HA). CASP3 has the canonical caspase prodomain-large subunit-small subunit architecture with catalytic C163 — preserve all elements. • Catalytically-dead rescue: C163A mutation in the catalytic cysteine abolishes proteolytic activity. • Constitutively active rescue: prodomain truncation generates revCASP3 with constitutive catalytic activity. • GSDME-uncleavable rescue: substrate-recognition mutations affecting GSDME D270 cleavage enable separation of apoptotic from pyroptotic functions. • Functional readout: rescue should restore PARP1 cleavage, apoptotic execution, and GSDME-mediated chemotherapy-induced pyroptosis. A-549 transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying CASP8 in lung cancer context for chemotherapy and TRAIL-targeted therapy research. The Knockout line is the standard tool for asking whether CASP8 is required for these processes in NSCLC context — CASP8 silencing/loss has been characterized in many cancers as an immune evasion and chemotherapy resistance mechanism; CASP8 status influences TRAIL-induced apoptosis. Overexpression is useful for studying CASP8 gain-of-function effects. For lung cancer apoptosis research, the EDITGENE CASP8 Knockout in A-549 is highly relevant. This product complements the parallel CASP8 Knockouts in L-02 (normal hepatocyte) and A-375 (BRAF melanoma) for cross-background validation. Rescue with wild-type or catalytically-dead CASP8 enables structure-function studies. The knockout is valuable for studying death receptor-induced apoptosis in NSCLC, TRAIL-targeted therapy resistance, and apoptosis-necroptosis switching in lung cancer biology.

Yes. CASP8 rescue experiments in A-549 are well-suited for lung cancer apoptosis research: • Construct design: same considerations as CASP8/L-02 rescue — preserve DED and protease domains. • Catalytically-dead C360S rescue: enables separation of proteolytic from scaffolding functions in NSCLC context. • Lung cancer mutation rescue: cancer-associated CASP8 mutations enable studies of CASP8 silencing in tumor biology. • Functional readout: rescue should restore TRAIL- and FAS-induced apoptosis in NSCLC context. A-549 transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying PD-L1 in a colorectal cancer context for MSI-H/dMMR cancer immunotherapy research. The Knockout line is the standard tool for asking whether PD-L1 is required for these processes in colorectal cancer context — HCT 116 is MSI-H (microsatellite instability-high), making this background highly relevant for PD-1/PD-L1 immunotherapy research since MSI-H/dMMR cancers are particularly responsive to anti-PD-1/PD-L1 therapy. Overexpression is useful for studying PD-L1 gain-of-function in colorectal context. For MSI-H colorectal cancer immunotherapy research, the EDITGENE CD274 Knockout in HCT 116 is uniquely valuable — pembrolizumab and nivolumab are FDA-approved for MSI-H/dMMR colorectal cancer (regardless of tissue of origin, FDA's first tissue-agnostic immunotherapy approval). This product complements the parallel CD274 Knockouts in HEK293 (biochemistry) and HeLa (imaging) for cross-background validation. Rescue with wild-type PD-L1 is the standard specificity control. The knockout is uniquely valuable for studying MSI-H/dMMR cancer immune evasion mechanisms and pembrolizumab/dostarlimab activity in colorectal cancer.

Yes. PD-L1 rescue in HCT 116 is well-suited for MSI-H cancer immunotherapy research: • Construct design: same considerations as PD-L1/HEK293 rescue. • Surface localization validation: confirm plasma membrane PD-L1 by cell surface staining. • MSI-H-context PD-L1 biology: rescue with WT PD-L1 enables systematic immune evasion mechanism studies in MSI-H CRC context. • Tissue-agnostic immunotherapy: pembrolizumab/dostarlimab specificity testing in MSI-H background. • Functional readout: rescue should restore PD-L1-dependent T cell suppression in CRC immunotherapy co-cultures. HCT 116 transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying B2M in melanoma context for checkpoint inhibitor resistance research. The Knockout line is the standard tool for asking whether B2M is required for these processes in BRAF V600E melanoma context — B2M loss is a documented mechanism of acquired resistance to anti-PD-1 (pembrolizumab/nivolumab) and anti-CTLA-4 (ipilimumab) in melanoma; landmark studies (Zaretsky et al. NEJM 2016; Sade-Feldman et al. Nat Commun 2017) identified B2M mutations in melanoma patients who relapsed after initial checkpoint inhibitor response. Overexpression is useful for studying B2M gain-of-function effects. For melanoma immunotherapy resistance research, the EDITGENE B2M Knockout in A-375 is uniquely valuable — A-375 is BRAF V600E-mutant melanoma, the principal melanoma model and the most clinically relevant context for B2M-mediated checkpoint inhibitor resistance. This product complements the parallel B2M Knockouts in HEK293T (biochemistry) and A-549 (lung cancer) for cross-background validation. The knockout is uniquely valuable for studying acquired checkpoint inhibitor resistance — one of the most clinically important problems in immunotherapy.

Yes. B2M rescue in A-375 is gold-standard for checkpoint inhibitor resistance research: • Construct design: same considerations as B2M/HEK293T rescue. • Melanoma anti-PD-1 response: WT B2M rescue restores MHC I-restricted melanoma neoantigen presentation and pembrolizumab/nivolumab-induced tumor killing. • Acquired resistance modeling: rescue with patient-derived B2M mutations (truncation, missense) enables on-target validation of B2M-mediated checkpoint inhibitor resistance. • Functional readout: rescue should restore HLA-ABC surface expression and melanoma neoantigen-specific CD8+ T cell recognition. A-375-specific considerations: • A-375 is a human melanoma cell line with BRAF V600E mutation — the principal in vitro model for BRAF-driven melanoma biology and BRAF/MEK inhibitor research. • Lentiviral transduction is supported with moderate efficiency. • MAPK pathway-driven cancer biology is the dominant feature of A-375.

The choice depends on whether you are studying BTRC (β-TrCP1, FBXW1)'s role as a major SCF E3 ligase substrate receptor or modeling its broad biological functions. The Knockout line is the standard tool for asking whether β-TrCP is required for these processes — BTRC is one of two β-TrCP paralogs (BTRC/FBXW1 and FBXW11/β-TrCP2) that serve as F-box substrate receptors in SCF^β-TrCP E3 ubiquitin ligase complexes; β-TrCP recognizes phosphodegron motifs (DSGxxS) on diverse substrates including IκBα (NF-κB signaling), β-catenin (Wnt signaling, recognized by both β-TrCP and APC pathways), Cdc25A (DNA damage response), Emi1, REST, and many others. Overexpression is useful for studying BTRC in heterologous expression contexts. Important consideration: BTRC and FBXW11/β-TrCP2 share substantial substrate scope — single BTRC knockout may show modest phenotypes if FBXW11 compensates. For ubiquitin biology research, the EDITGENE BTRC Knockout in HeLa enables study of β-TrCP1-specific functions. Rescue with wild-type or substrate-binding-deficient BTRC is the standard specificity control. The knockout is valuable for studying NF-κB activation (IκBα degradation), Wnt signaling (β-catenin degradation), DNA damage response (Cdc25A degradation), and emerging targeted protein degradation approaches using β-TrCP-recruiting PROTACs.

Yes. BTRC rescue experiments require attention to F-box substrate receptor architecture: • Construct design: use a codon-modified BTRC sequence with a small C-terminal tag (FLAG, HA). BTRC has N-terminal F-box domain (SKP1 binding) and C-terminal WD40 domain (substrate phosphodegron binding) — preserve all elements. • Substrate-binding-deficient rescue: WD40 domain mutations disrupt phosphodegron substrate binding. • F-box-deficient rescue: F-box mutations disrupt SCF complex assembly. • Functional readout: rescue should restore IκBα/β-catenin/Cdc25A degradation. HeLa transduces efficiently with lentivirus and supports stable rescue line generation.