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ACVR2A and ACVR2B are the two type II activin receptors — serine/threonine kinase receptors that bind activins, myostatin (GDF8), GDF11, BMPs, and other TGF-β superfamily ligands; upon ligand binding, the type II receptor recruits and phosphorylates type I receptors (ALK4/ACVR1B, ALK5, ALK7), which then phosphorylate SMAD2/3 (activin/myostatin branch) to regulate gene expression. ACVR2A and ACVR2B share substantial ligand and functional overlap, with myostatin/GDF11-mediated muscle growth suppression being a major shared function. This ligand-trap axis is the basis of several clinically important therapeutics. The choice between knockout and overexpression depends on whether you are studying ACVR2A in the HAP1 haploid platform for systematic genetic analysis. This ACVR2A Knockout in HAP1 enables study of ACVR2A-specific functions in a clean haploid background. Overexpression is useful for studying ACVR2A gain-of-function effects. Important consideration: ACVR2B paralog expression analysis aids interpretation given substantial functional overlap. This product complements the parallel ACVR2A Knockout in HEK293 and the ACVR2A & ACVR2B Double Knockout in HEK293 (both also available) for systematic cross-background paralog dissection. Rescue with wild-type or kinase-dead ACVR2A is the standard specificity control. The knockout is valuable for studying activin/myostatin type II receptor biology and as a specificity tool for sotatercept/luspatercept/bimagrumab-class ligand traps. 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.

Yes. ACVR2A rescue in HAP1 follows the same considerations as the HEK293 product: • Construct design: same considerations as ACVR2A/HEK293 rescue (kinase domain preservation, intracellular C-terminal tag, surface localization validation). • Kinase-dead rescue: K219R mutation abolishes catalytic activity. • Cross-background validation: parallel rescue in HAP1 and HEK293 confirms ACVR2A-specific phenotypes. • Functional readout: rescue should restore activin/myostatin-induced phospho-SMAD2/3. 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 ANXA1 (annexin A1, lipocortin 1)'s role as a pro-resolving anti-inflammatory mediator or modeling its functions in cancer biology. The Knockout line is the standard tool for asking whether ANXA1 is required for these processes — ANXA1 is a Ca²⁺/phospholipid-binding protein that, upon cellular stress or glucocorticoid stimulation, is released to the extracellular space where it binds formyl peptide receptors (FPR2/ALX, FPR1) on neutrophils and monocytes, mediating inflammation resolution; ANXA1 is a major effector of glucocorticoid anti-inflammatory effects. Overexpression is useful for studying ANXA1 gain-of-function effects. For inflammation resolution research, the EDITGENE ANXA1 Knockout in HAP1 enables study of ANXA1 biology. Other annexin family members (ANXA2, ANXA5, ANXA6) expression analysis aids interpretation. Rescue with wild-type ANXA1 is the standard specificity control. The knockout is valuable for studying glucocorticoid anti-inflammatory mechanisms, neutrophil/monocyte resolution biology, FPR2/ALX agonism (emerging ANXA1-mimetic peptides Ac2-26, BMS-986235 in clinical development for cardiovascular and inflammatory diseases), and emerging ANXA1 functions in cancer biology.

Yes. ANXA1 rescue experiments are well-established for inflammation resolution research: • Construct design: use a codon-modified ANXA1 sequence with a small C-terminal tag (FLAG, HA). ANXA1 has N-terminal regulatory region (Ac2-26 mimetic peptide region) and C-terminal annexin core domain (Ca²⁺/phospholipid binding) — preserve all elements. • FPR2-binding-deficient rescue: N-terminal mutations disrupt FPR2/ALX agonism. • Cleavage-site mutants: ANXA1 N-terminal cleavage site mutations affect Ac2-26-like peptide generation. • Functional readout: rescue should restore glucocorticoid-induced ANXA1 release and FPR2-mediated resolution signaling. 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 PHGDH (phosphoglycerate dehydrogenase)'s role as the rate-limiting enzyme of de novo serine biosynthesis or modeling its applications in cancer metabolism and porcine biology. The Knockout line is the standard tool for asking whether PHGDH is required for these processes — PHGDH catalyzes the first and rate-limiting step of the serine synthesis pathway (SSP), oxidizing 3-phosphoglycerate (from glycolysis) to 3-phosphohydroxypyruvate using NAD⁺ as cofactor; downstream PSAT1 and PSPH complete serine biosynthesis. Serine is a major one-carbon donor (through SHMT1/2-mediated conversion to glycine and methylenetetrahydrofolate), supporting nucleotide synthesis, methylation reactions, redox homeostasis (GSH synthesis), and lipid biosynthesis. Overexpression is useful for studying PHGDH gain-of-function effects. For cancer metabolism research, the EDITGENE PHGDH Knockout in PK-15 is uniquely valuable — PHGDH genomic amplification has been characterized in ⭐⭐ basal-like/triple-negative breast cancer (~6%) and melanoma, where it drives serine auxotrophy escape and is an established cancer metabolism target; PHGDH is a leading 'metabolic oncogene' candidate. Rescue with wild-type or catalytically-dead PHGDH enables structure-function studies. The knockout is a critical specificity tool for ⭐ PHGDH-selective inhibitors (NCT-503, CBR-5884, WQ-2101, and emerging compounds in preclinical/clinical development), serine deprivation cancer therapy research, and emerging PHGDH-related porcine biology (PHGDH is also important for skeletal muscle and embryonic development). PK-15-specific considerations: • PK-15 (CCL-33) is a porcine (Sus scrofa) kidney epithelial cell line widely used in veterinary virology as a primary host for porcine circovirus (PCV2), classical swine fever virus (CSFV), pseudorabies virus (PRV), porcine parvovirus, and other swine pathogens. • Lentiviral transduction is supported with moderate efficiency, but optimization may be required compared to standard human immortalized lines. • PK-15 cells contain endogenous porcine type C retrovirus (PERV) particles and are reported to be persistently positive for PCV2 antigens — these features should be considered when designing viral immunology and xenotransplantation-relevant experiments. • PK-15 cells retain intact type I IFN signaling (unlike Vero cells), making them suitable for innate immunity studies but potentially limiting for some virus isolation workflows. • PK-15 cell clones with differing virus permissivity have been characterized — phenotypic heterogeneity should be assessed before key experiments.

Yes. PHGDH rescue experiments are well-established for serine biosynthesis research: • Construct design: use a codon-modified PHGDH sequence with a small C-terminal tag (FLAG, HA). PHGDH has the canonical D-2-hydroxyacid dehydrogenase architecture with N-terminal substrate-binding domain, central NAD-binding Rossmann fold, and C-terminal ACT regulatory domain (serine feedback inhibition site) — preserve all elements. • Catalytically-dead rescue: active site mutations (catalytic His or Glu) abolish PHGDH activity. • Feedback-resistant rescue: ACT domain mutations disrupt serine feedback inhibition, generating constitutively active PHGDH. • Species considerations: porcine PHGDH (NCBI ID 100144529) and human PHGDH share substantial homology; either species cDNA can be used for rescue with appropriate species-matching for in vivo veterinary studies. • Functional readout: rescue should restore serine prototrophy and 13C-glucose-traced serine synthesis. PK-15-specific considerations: • PK-15 (CCL-33) is a porcine (Sus scrofa) kidney epithelial cell line widely used in veterinary virology as a primary host for porcine circovirus (PCV2), classical swine fever virus (CSFV), pseudorabies virus (PRV), porcine parvovirus, and other swine pathogens. • Lentiviral transduction is supported with moderate efficiency, but optimization may be required compared to standard human immortalized lines. • PK-15 cells contain endogenous porcine type C retrovirus (PERV) particles and are reported to be persistently positive for PCV2 antigens — these features should be considered when designing viral immunology and xenotransplantation-relevant experiments. • PK-15 cells retain intact type I IFN signaling (unlike Vero cells), making them suitable for innate immunity studies but potentially limiting for some virus isolation workflows. • PK-15 cell clones with differing virus permissivity have been characterized — phenotypic heterogeneity should be assessed before key experiments.

The choice depends on whether you are studying ALOX12 (platelet-type 12-lipoxygenase, 12-LOX)'s role as the principal 12-HETE-generating enzyme or modeling its functions in platelet biology, ferroptosis, and emerging cancer applications. The Knockout line is the standard tool for asking whether 12-LOX is required for these processes — ALOX12 catalyzes the conversion of arachidonic acid to 12(S)-HPETE/12(S)-HETE; ALOX12 is highly expressed in platelets where 12-HETE contributes to platelet activation, and has emerging roles in ferroptosis (12-LOX-generated lipid peroxides drive iron-dependent cell death). Overexpression is useful for studying ALOX12 gain-of-function effects. Important consideration: ALOX12 (12S-LOX) is distinct from ALOX12B (12R-LOX, epidermal); these enzymes generate stereochemically opposite products from arachidonic acid. For platelet and ferroptosis research, the EDITGENE ALOX12 Knockout in HAP1 enables study of 12S-LOX biology. This product complements the parallel ALOX12B Knockout in HEK293 (also available, epidermal isoform) for stereochemistry dissection. Rescue with wild-type or catalytically-dead ALOX12 enables structure-function studies. The knockout is a critical specificity tool for ⭐ ML355 (selective ALOX12 inhibitor), and emerging ferroptosis-targeted and platelet-targeted therapeutics.

Yes. ALOX12 rescue experiments are well-established for lipoxygenase research: • Construct design: use a codon-modified ALOX12 sequence with a small C-terminal tag (FLAG, HA). ALOX12 has the canonical lipoxygenase architecture with active site iron — preserve all elements. • Catalytically-dead rescue: iron-binding histidine cluster mutations abolish 12-LOX activity. • ML355-resistant rescue: gatekeeper mutations can confer ML355 resistance for on-target validation. • Functional readout: rescue should restore 12(S)-HETE generation from arachidonic acid. 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.

AKT (Protein Kinase B) is a family of three paralogous serine/threonine kinases (AKT1/PKBα, AKT2/PKBβ, AKT3/PKBγ) that are activated downstream of PI3K signaling — PI3K generates PIP3, which recruits AKT to the plasma membrane via its PH domain; AKT is then phosphorylated at T308 (activation loop, by PDK1) and S473 (hydrophobic motif, by mTORC2) for full activation. AKT family members share substantial substrate scope but have distinct tissue expression and functions: AKT1 is broadly expressed and important in cell survival/growth; AKT2 is enriched in insulin-sensitive tissues (liver, muscle, adipose) and central to insulin signaling; AKT3 is enriched in brain and testis with roles in neural development. Substantial paralog redundancy means that single-isoform knockouts often show modest phenotypes — paired and combination knockouts are essential for systematic functional dissection. This AKT1 & AKT2 Double Knockout in A-549 is uniquely valuable for asking which functions are AKT1/AKT2-dependent versus AKT3-dependent — combined loss of AKT1 and AKT2 leaves only AKT3 as the functional AKT isoform; AKT3 is principally expressed in brain and testis, making AKT3-only cells particularly suited to neural-relevant signaling research. Single-isoform rescue (AKT1 alone or AKT2 alone) in the double knockout enables paralog-specific functional dissection. For systematic AKT family research, this product is part of EDITGENE's complete AKT paralog dissection toolkit. The AKT1&AKT2 double KO removes the two principal AKT isoforms (~95% of total AKT signaling in most non-neural contexts), enabling clean AKT3-only signaling analysis. The knockout is uniquely valuable for studying brain-relevant AKT3 functions in heterologous A-549 background.

Yes, and rescue experiments are uniquely powerful in this AKT1&2 double knockout: • Single-isoform rescue: re-introduction of AKT1 alone or AKT2 alone enables paralog-specific dissection. • AKT3-only signaling: this double KO is the cleanest model for AKT3-specific functions (brain-relevant). • Construct design: same considerations as AKT family rescues. • Functional readout: rescue should restore PI3K-AKT signaling. A-549-specific considerations: • A-549 is a human non-small cell lung carcinoma (NSCLC) cell line widely used for lung cancer drug development. • Lentiviral transduction is supported with moderate efficiency. • A-549's PI3K-AKT pathway activity makes it a relevant context for systematic AKT paralog research.

AKT (Protein Kinase B) is a family of three paralogous serine/threonine kinases (AKT1/PKBα, AKT2/PKBβ, AKT3/PKBγ) that are activated downstream of PI3K signaling — PI3K generates PIP3, which recruits AKT to the plasma membrane via its PH domain; AKT is then phosphorylated at T308 (activation loop, by PDK1) and S473 (hydrophobic motif, by mTORC2) for full activation. AKT family members share substantial substrate scope but have distinct tissue expression and functions: AKT1 is broadly expressed and important in cell survival/growth; AKT2 is enriched in insulin-sensitive tissues (liver, muscle, adipose) and central to insulin signaling; AKT3 is enriched in brain and testis with roles in neural development. Substantial paralog redundancy means that single-isoform knockouts often show modest phenotypes — paired and combination knockouts are essential for systematic functional dissection. This AKT1 & AKT3 Double Knockout in A-549 is uniquely valuable for asking which functions are AKT1/AKT3-dependent versus AKT2-dependent — combined loss of AKT1 and AKT3 leaves only AKT2 as the functional AKT isoform, which is particularly useful for isolating AKT2-mediated insulin signaling. Single-isoform rescue (AKT1 alone or AKT3 alone) in the double knockout enables paralog-specific functional dissection. For systematic AKT family research, this product is part of EDITGENE's complete AKT paralog dissection toolkit. The double KO enables clean AKT2-only signaling analysis. The knockout is a critical specificity tool for capivasertib (Truqap), ipatasertib, MK-2206, ARQ-092, and isoform-selective emerging AKT inhibitors.

Yes, and rescue experiments are uniquely powerful in this AKT1&3 double knockout: • Single-isoform rescue: re-introduction of AKT1 alone or AKT3 alone enables paralog-specific dissection. • Construct design: same considerations as AKT family rescues. • AKT1 E17K rescue: cancer-associated AKT1 E17K activating mutation enables HR+ breast cancer disease modeling. • Functional readout: rescue should restore PI3K-AKT signaling. A-549-specific considerations: • A-549 is a human non-small cell lung carcinoma (NSCLC) cell line widely used for lung cancer drug development. • Lentiviral transduction is supported with moderate efficiency. • A-549's PI3K-AKT pathway activity makes it a relevant context for systematic AKT paralog research.

AKT (Protein Kinase B) is a family of three paralogous serine/threonine kinases (AKT1/PKBα, AKT2/PKBβ, AKT3/PKBγ) that are activated downstream of PI3K signaling — PI3K generates PIP3, which recruits AKT to the plasma membrane via its PH domain; AKT is then phosphorylated at T308 (activation loop, by PDK1) and S473 (hydrophobic motif, by mTORC2) for full activation. AKT family members share substantial substrate scope but have distinct tissue expression and functions: AKT1 is broadly expressed and important in cell survival/growth; AKT2 is enriched in insulin-sensitive tissues (liver, muscle, adipose) and central to insulin signaling; AKT3 is enriched in brain and testis with roles in neural development. Substantial paralog redundancy means that single-isoform knockouts often show modest phenotypes — paired and combination knockouts are essential for systematic functional dissection. This AKT2 & AKT3 Double Knockout in A-549 is uniquely valuable for asking which functions are AKT1-dependent versus AKT2/AKT3-dependent — combined loss of AKT2 and AKT3 leaves only AKT1 as the functional AKT isoform. Single-isoform rescue (AKT2 alone or AKT3 alone) in the double knockout enables paralog-specific functional dissection — this is the gold-standard experimental design for AKT paralog studies. For systematic AKT family research, the EDITGENE AKT2 & AKT3 Double Knockout in A-549 is part of a complete EDITGENE AKT paralog dissection toolkit (single AKT1, single AKT2, double AKT1&AKT2, double AKT1&AKT3, double AKT2&AKT3 — all in A-549 NSCLC background). This systematic matrix enables comprehensive AKT family functional analysis. The knockout is a critical specificity tool for ⭐⭐ capivasertib (Truqap, FDA-approved 2023 pan-AKT inhibitor for HR+/HER2− breast cancer with PIK3CA/AKT1/PTEN alterations), ipatasertib, MK-2206 (allosteric AKT inhibitor), ARQ-092/miransertib, and isoform-selective emerging AKT inhibitors.

Yes, and rescue experiments are uniquely powerful in this AKT2&3 double knockout: • Single-isoform rescue: ⭐ re-introduction of AKT2 alone or AKT3 alone enables paralog-specific dissection — gold-standard experimental design. • Construct design: use codon-modified AKT2 or AKT3 sequences with small C-terminal tags (FLAG, HA) — preserve PH domain, kinase domain, and regulatory C-terminus. • Kinase-dead rescue: K181M (AKT2) or K177M (AKT3) ATP-binding lysine mutations abolish catalytic activity. • Constitutively active rescue: myristoylated AKT (myr-AKT) constitutive plasma membrane localization generates active AKT without PI3K input. • Functional readout: rescue should restore PI3K-AKT signaling measured by phospho-substrates (GSK3β S9, FOXO1 T24, S6K T389). A-549-specific considerations: • A-549 is a human non-small cell lung carcinoma (NSCLC) cell line widely used for lung cancer drug development. • Lentiviral transduction is supported with moderate efficiency. • A-549's PI3K-AKT pathway activity makes it a relevant context for systematic AKT paralog research.

We complement missing amino acids at the cut site and prioritize insertion in non-critical domains (e.g., via flexible linkers) or 3'UTR; a "self-cleaving peptide" (P2A/T2A) strategy is also available to co-express tag and protein without fusion.