Contact Us

The choice depends on whether you are studying BNIP3's role as a mitophagy receptor or modeling its functions in hypoxia-induced autophagy and cell death. The Knockout line is the standard tool for asking whether BNIP3 is required for these processes — BNIP3 is a BH3-only Bcl-2 family member with C-terminal mitochondrial membrane targeting that functions as a hypoxia-induced (HIF1α-target) mitophagy receptor; BNIP3 contains an LC3-interacting region (LIR motif) that recruits LC3-positive autophagosomes to mitochondria for selective degradation; BNIP3 also has roles in necroptosis and Bax/Bak-mediated cell death. Overexpression is useful for studying BNIP3 gain-of-function effects. Important consideration: BNIP3L/NIX paralog expression analysis aids interpretation given functional overlap. For mitophagy and hypoxia research, the EDITGENE BNIP3 Knockout in HeLa enables study of receptor-mediated mitophagy. Rescue with wild-type or LIR-mutant BNIP3 (W18A/L21A in LIR motif) enables structure-function studies. The knockout is valuable for studying hypoxia-induced mitophagy, mitochondrial quality control, and emerging BNIP3-related cancer biology.

Yes. BNIP3 rescue experiments require attention to mitochondrial outer membrane targeting: • Construct design: use a codon-modified BNIP3 sequence with a small N-terminal tag (FLAG, HA) — BNIP3 has N-terminal cytosolic regions and C-terminal transmembrane domain for MOM targeting; N-terminal tag preserves the LIR motif (residues 17-21) and transmembrane region. • Mitochondrial outer membrane localization validation: confirm MOM localization before mitophagy assays. • LIR-mutant rescue: W18A/L21A mutations in the LIR motif abolish LC3 binding and mitophagy receptor function. • BH3-deficient rescue: BH3 domain mutations affect Bax/Bak interactions. • Functional readout: rescue should restore hypoxia-induced mitophagy measured by mt-Keima reporter. HeLa transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying CDKN1B (p27^Kip1)'s role as a Cip/Kip family cyclin-dependent kinase inhibitor or modeling its functions in lung cancer cell cycle regulation. The Knockout line is the standard tool for asking whether p27 is required for these processes — CDKN1B/p27 is a CDK inhibitor that binds and inhibits Cyclin E-CDK2 and Cyclin A-CDK2 complexes (G1/S transition), with paradoxical assembly/activating roles for Cyclin D-CDK4/6; p27 is regulated by phosphorylation (S10, T187 destruction signal, T157/T198 cytoplasmic relocalization) and by SCF^SKP2-mediated degradation. Overexpression is useful for studying p27 gain-of-function effects. For lung cancer research, the EDITGENE CDKN1B Knockout in A-549 is highly relevant — A-549 is an NSCLC cell line, and p27 loss is a common cancer event (often via post-translational mechanisms rather than gene deletion). Rescue with wild-type or T187A (SKP2-resistant, stable) p27 enables structure-function and cancer modeling studies. The knockout is valuable for studying CDK inhibition biology, Cyclin E-CDK2-mediated G1/S progression, and emerging p27-stabilizing approaches in cancer.

Yes. p27 rescue experiments are well-established for cell cycle research: • Construct design: use a codon-modified CDKN1B sequence with a small C-terminal tag (FLAG, HA). p27 has N-terminal CDK inhibitor (CKI) domain, central QT region with T187 destruction signal, and C-terminal regions — preserve all elements. • T187A stable rescue: T187A mutation prevents SCF^SKP2-mediated degradation, generating stable p27 with prolonged G1 arrest activity. • T157A/T198A cytoplasmic-deficient rescue: T157A and T198A mutations prevent AKT-mediated cytoplasmic relocalization. • CDK-binding-deficient rescue: CKI domain mutations disrupt Cyclin-CDK binding without affecting other p27 functions. • Functional readout: rescue should restore G1 arrest and Cyclin E-CDK2 inhibition. A-549 transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying AXL's role as a TAM (TYRO3-AXL-MERTK) family receptor tyrosine kinase or modeling its emerging functions as a cancer drug resistance and immunotherapy target. The Knockout line is the standard tool for asking whether AXL is required for these processes — AXL is activated by GAS6 ligand binding (also PROS1); AXL is critical for efferocytosis (apoptotic cell clearance), epithelial-mesenchymal transition (EMT), and has emerged as a major mediator of resistance to EGFR-TKIs, chemotherapy, and immunotherapy in lung and other cancers. Overexpression is useful for studying AXL gain-of-function effects. For NSCLC drug resistance research, the EDITGENE AXL Knockout in A-549 is uniquely valuable — AXL upregulation is a key mechanism of acquired resistance to osimertinib and other EGFR-TKIs in EGFR-mutated NSCLC. Rescue with wild-type or kinase-dead AXL is the standard specificity control. The knockout is a critical specificity tool for ⭐⭐ bemcentinib (BGB324, AVB-500, AXL-selective inhibitor in NSCLC and AML clinical development), enapotamab vedotin (anti-AXL ADC), TP-0903, and emerging AXL-targeted therapeutics — AXL is one of the most validated cancer drug resistance targets.

Yes. AXL rescue experiments are well-established for cancer drug resistance research: • Construct design: use a codon-modified AXL sequence with a small intracellular C-terminal tag (FLAG, HA). AXL has extracellular Ig and FN3 domains (GAS6 binding), transmembrane span, and intracellular kinase domain — preserve all elements. • Surface localization validation: confirm plasma membrane localization before GAS6 binding studies. • Kinase-dead rescue: K567R mutation in the ATP-binding lysine abolishes catalytic activity. • Bemcentinib-resistant rescue: gatekeeper mutations can confer bemcentinib resistance for on-target validation. • Functional readout: rescue should restore GAS6-induced phospho-AXL and downstream signaling. A-549 transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on the experimental question. CCNL2 (cyclin L2) is a less-characterized cyclin family member with characterized roles in splicing factor regulation. The Knockout line is appropriate for asking whether CCNL2 is required for predicted activities — CCNL2 is paralog of CCNL1 with characterized roles as a partner of cyclin-dependent kinases CDK11 and CDK12 in splicing factor phosphorylation and RNA processing. Overexpression is useful for studying CCNL2 in heterologous expression contexts. For RNA processing research, the EDITGENE CCNL2 Knockout in HeLa provides a clean genetic background for characterizing CCNL2-specific functions. CCNL1 paralog expression analysis aids interpretation. Rescue with wild-type CCNL2 is the standard specificity control. The knockout is valuable for studying less-characterized cyclin L biology and emerging CDK11/CDK12-CCNL pathway research.

Yes. CCNL2 rescue experiments require attention to cyclin architecture: • Construct design: use a codon-modified CCNL2 sequence with a small C-terminal tag (FLAG, HA). CCNL2 has cyclin-box domains — preserve protein integrity. • CDK-binding-deficient rescue: cyclin-box mutations disrupt CDK11/CDK12 binding. • Functional readout: rescue should restore CCNL2-dependent splicing factor phosphorylation and alternative splicing patterns. HeLa transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying CERT1 (ceramide transfer protein 1, COL4A3BP, STARD11)'s role as a non-vesicular ceramide transporter or modeling its functions in sphingolipid biology and emerging neurodevelopmental disease. The Knockout line is the standard tool for asking whether CERT1 is required for these processes — CERT1 is a START-domain containing protein that mediates non-vesicular transfer of ceramide from the ER to the trans-Golgi network for sphingomyelin and glucosylceramide synthesis; CERT1 has N-terminal PH domain (Golgi PI4P binding), middle FFAT motif (ER VAP binding), and C-terminal START domain (ceramide binding). Overexpression is useful for studying CERT1 in heterologous expression contexts. For sphingolipid biology research, the EDITGENE CERT1 Knockout in HeLa is highly informative — CERT1 de novo heterozygous mutations cause autosomal dominant intellectual disability syndrome (NEDMIAH, neurodevelopmental disorder with intellectual disability and seizures). Rescue with wild-type, ceramide-binding-deficient (G67E START domain), or NEDMIAH-associated CERT1 mutations enables comprehensive structure-function and disease modeling. The knockout is valuable for studying ER-Golgi non-vesicular lipid transfer and CERT1-related neurodevelopmental disorder mechanisms.

Yes. CERT1 rescue experiments are well-established for non-vesicular lipid transfer research: • Construct design: use a codon-modified CERT1 sequence with a small C-terminal tag (FLAG, HA). CERT1 has N-terminal PH domain (Golgi PI4P binding), middle FFAT motif (ER VAP-A/B binding), and C-terminal START domain (ceramide binding) — preserve all elements. • Ceramide-binding-deficient rescue: G67E mutation in the START domain abolishes ceramide binding. • PH-deficient rescue: PH domain mutations disrupt Golgi PI4P binding. • FFAT-mutant rescue: FFAT motif mutations disrupt ER VAP binding. • NEDMIAH mutation rescue: de novo heterozygous CERT1 mutations enable disease modeling. • Functional readout: rescue should restore ER-Golgi ceramide transfer and sphingomyelin synthesis. HeLa transduces efficiently with lentivirus and supports stable rescue line generation.

The choice depends on whether you are studying CD274 (PD-L1)'s role as the principal immune checkpoint ligand or modeling PD-L1-targeted cancer immunotherapy in imaging-friendly context. The Knockout line is the standard tool for asking whether PD-L1 is required for these processes — PD-L1 (CD274, B7-H1) is the principal ligand for PD-1 (PDCD1) on activated T cells; PD-L1-PD-1 engagement transduces inhibitory signaling through PD-1 ITSM motifs, recruiting SHP1/SHP2 to dephosphorylate TCR signaling components and dampen T cell activation; PD-L1 is constitutively expressed at low levels and dramatically upregulated by IFN-γ via JAK-STAT-IRF1 signaling; PD-L1 expression on tumor cells is a major immune evasion mechanism. Overexpression is useful for studying PD-L1 gain-of-function effects. For PD-L1 cancer immunotherapy research, the EDITGENE CD274 Knockout in HeLa is uniquely valuable — HeLa's flat morphology supports imaging-based PD-L1 trafficking studies. This product complements the parallel CD274 Knockouts in HEK293 (biochemistry) and HCT 116 (colorectal context) for cross-background validation. Rescue with wild-type or trafficking-deficient PD-L1 enables structure-function studies. The knockout is a critical specificity control for ⭐⭐⭐ all PD-L1-targeted therapies: ⭐⭐⭐ atezolizumab (Tecentriq), durvalumab (Imfinzi), avelumab (Bavencio), and the anti-PD-1 antibodies that target the PD-L1 partner — pembrolizumab (Keytruda, top-selling cancer drug), nivolumab (Opdivo), cemiplimab (Libtayo); also CMTM6-targeted approaches (CMTM6 stabilizes PD-L1).

Yes. PD-L1 rescue experiments are well-established for cancer immunotherapy research: • Construct design: use a codon-modified CD274 sequence with a small intracellular C-terminal tag (FLAG, HA). PD-L1 is a type I membrane protein with extracellular IgV and IgC2 domains (PD-1 binding), transmembrane span, and short cytoplasmic tail — preserve membrane topology. • Surface localization validation: confirm plasma membrane PD-L1 by cell surface staining (anti-PD-L1 antibody clones 28-8, SP142, 22C3, SP263) before functional assays. • PD-1-binding-deficient rescue: IgV domain mutations abolish PD-1 binding while preserving surface expression. • Functional readout: rescue should restore IFN-γ-inducible PD-L1 expression and anti-PD-L1 antibody/anti-PD-1 antibody activity in PD-1-expressing T cell co-cultures. HeLa transduces efficiently with lentivirus and supports stable rescue line generation for systematic PD-L1 imaging studies.

The choice depends on whether you are studying CRBN (cereblon)'s role as the substrate receptor of the CRL4^CRBN E3 ubiquitin ligase or modeling the foundational platform for IMiD drugs and molecular glue degraders — CRBN is one of the most clinically validated cancer drug targets and the original molecular glue degrader receptor. The Knockout line is the gold-standard tool for asking whether CRBN is required for these processes — CRBN is a CUL4-RING E3 ligase substrate receptor (with DDB1, CUL4A, RBX1 forming CRL4^CRBN) that was identified as the molecular target of thalidomide (the cause of historical birth defects); structural studies revealed that thalidomide and its analogs (IMiDs: lenalidomide, pomalidomide) bind CRBN and recruit neo-substrates (IKZF1, IKZF3, CK1α, GSPT1) for polyubiquitination and proteasomal degradation. This is the prototypical 'molecular glue' mechanism. Overexpression is useful for studying CRBN in heterologous expression contexts. For targeted protein degradation research, the EDITGENE CRBN Knockout in HeLa is uniquely valuable — CRBN is the foundational and most clinically validated target of the entire molecular glue and PROTAC field. Rescue with wild-type or thalidomide-binding-pocket mutant (Y355A, W380A — the critical thalidomide-binding tri-tryptophan pocket; or Y386A — Y384 in some numbering) CRBN enables systematic IMiD/molecular glue/PROTAC specificity testing. The knockout is a critical specificity control for ⭐⭐⭐ thalidomide (Thalomid), ⭐⭐⭐ lenalidomide (Revlimid, top-selling multiple myeloma drug), ⭐⭐⭐ pomalidomide (Pomalyst), iberdomide (Iberlumate/CC-220), mezigdomide (CC-92480), CC-90009 (GSPT1 degrader), and the entire class of CRBN-recruiting PROTACs (ARV-110/bavdegalutamide for prostate cancer, ARV-471/vepdegestrant for ER+ breast cancer, KT-474 for IRAK4 in atopic dermatitis/hidradenitis suppurativa, NX-2127 for BTK). CRBN-recruiting molecular glue degraders and PROTACs constitute one of the most rapidly growing classes of cancer drugs.

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 (HBD), and C-terminal thalidomide-binding domain (TBD) with the critical tri-tryptophan pocket (W380, W386, W400, plus Y355) — preserve all elements. • Thalidomide-binding-pocket mutant rescue: ⭐⭐ Y355A, W380A, W386A, W400A mutations in the tri-tryptophan/Y-pocket abolish IMiD binding and serve as the gold-standard specificity control — these mutations distinguish CRBN-dependent from CRBN-independent compound activities. • IMiD resistance mutation rescue: rescue with patient-derived CRBN mutations from IMiD-resistant multiple myeloma (e.g., A395, Y384 missense, frameshift mutations) for clinical resistance mechanism studies. • DDB1-binding-deficient rescue: N-terminal CRBN mutations disrupt CRL4 complex assembly. • Functional readout: rescue should restore IKZF1, IKZF3, CK1α degradation upon lenalidomide treatment; thalidomide-binding-pocket mutants should be insensitive to all IMiDs and CRBN-recruiting molecular glues. HeLa transduces efficiently with lentivirus and supports systematic CRBN mutation analysis for the entire CRBN-targeted therapeutic field — this is one of the most important genetic tools in modern cancer drug development.

The choice depends on whether you are studying CBS (cystathionine β-synthase)'s role as the initiating enzyme of transsulfuration and a major H₂S-generating enzyme or modeling homocystinuria. The Knockout line is the standard tool for asking whether CBS is required for these processes — CBS catalyzes the first step of transsulfuration (homocysteine + serine → cystathionine), committing methionine-derived homocysteine to cysteine biosynthesis; CBS is one of three principal H₂S-generating enzymes (with CTH/CSE and 3-MST/MPST), and CBS uses pyridoxal-5'-phosphate (PLP, vitamin B6 derivative) as cofactor. Overexpression is useful for studying CBS gain-of-function effects. For transsulfuration and H₂S biology research, the EDITGENE CBS Knockout in HEK293 enables study of CBS biology. This product complements the parallel CTH Knockout in A-549 (also available) for complete transsulfuration axis dissection — CBS catalyzes the first step (homocysteine → cystathionine), while CTH catalyzes the second step (cystathionine → cysteine + H₂S). CBS biallelic loss-of-function causes ⭐ classical homocystinuria (autosomal recessive, often pyridoxine-responsive due to PLP cofactor); pyridoxine therapy ameliorates ~50% of patients. Rescue with wild-type or PLP-binding-deficient CBS enables structure-function studies. The knockout is valuable for studying homocystinuria mechanisms and emerging CBS-targeted therapeutics — ⭐ pegtibatinase/EnzymeRx OT-58 enzyme replacement (in Phase III for classical homocystinuria) is an emerging therapy.