ced-7 encodes a C. elegans ABC transporter of the A subfamily, related to mammalian ABCA1. CED-7 is required both on the dying cell (for phosphatidylserine exposure) and on the engulfing cell (for corpse recognition), making it a unique dual-function component of the engulfment pathway.
ABCA1 is the gene mutated in Tangier disease and a central controller of cellular lipid homeostasis. CD BioSciences designs and delivers custom ced-7 alleles — knockout, knockin, and ATPase-domain point mutants — for ABC transporter and atherosclerosis research.
| Gene symbol | ced-7 (ABC transporter (engulfment)) |
|---|---|
| Protein product | CED-7 — ABCA1-like transporter |
| Mammalian homolog | ABCA1 (and related ABC-A subfamily) |
| Biological role | ABC transporter required for phosphatidylserine exposure on apoptotic cells and for the recognition step of corpse clearance on the engulfing-cell side. |
| Loss-of-function phenotype | Persistent cell corpses; engulfment-defective on both the dying-cell and engulfing-cell sides. |
| Why edit it | ABCA1 in cholesterol efflux and atherosclerosis (Tangier disease); lipid asymmetry; cell-cell recognition in phagocytosis. |
| Recommended background | N2 (wild type); can be combined with ced-1, ced-6, or ced-10 mutants. |
| Representative allele | Standard knockout (ok / tm / gk series); n1994 is a canonical reference allele. |
ced-7 at a glance: blocks engulfment of apoptotic corpses; persistent-cell-corpse phenotype easy to score. Editing ced-7 alone is a powerful way to dissect CED-7 function in vivo, with conserved relevance to human ABCA1 biology.
gRNA-guided Cas9 cutting with NHEJ repair to introduce frameshift indels, generating premature stop codons and null / strong-loss-of-function ced-7 alleles.
Homology-directed repair (HDR) inserts GFP / HA / FLAG or other tags at the ced-7 locus for endogenous expression and subcellular localization studies.
Introduce specific amino-acid substitutions to dissect functional domains and separate catalytic from scaffolding roles of CED-7.
Build tissue-specific or inducible configurations and reporter lines for spatiotemporal analysis of CED-7 function.
Define target (knockout / knockin / point mutation), select gRNA(s) and HDR template, confirm against the latest genome build.
Design, validate, and synthesize high-specificity guide RNAs targeting the ced-7 locus.
Build Cas9 / gRNA delivery construct and, for knockin, the homology-arm repair template.
Perform gonadal microinjection of N2 animals with CRISPR components and co-CRISPR selection markers.
PCR, Sanger / sequencing, and phenotype confirmation to isolate edited animals and verify alleles.
Provide homozygous / balanced ced-7 strains plus a full genotype and methods report.
Standard knockout projects deliver a frameshift indel allele predicted to produce a premature stop and a loss-of-function phenotype. We confirm the edit by sequencing and, where relevant, by characteristic phenotype assays.
Yes. Using HDR with a designed repair template, we can insert GFP, HA, or FLAG tags at the C- or N-terminus while preserving endogenous promoter and regulation.
Timelines vary with editing type and validation needs, but our optimized pipeline and co-CRISPR selection typically shorten turnaround versus conventional approaches. Contact us with your design for a project-specific estimate.
Both. CED-7 is required on the apoptotic cell for phosphatidylserine exposure and on the engulfing cell for corpse recognition. Mosaic analysis is the standard way to dissect the two roles, and our knockin / knockout alleles are well suited to such experiments.
CD BioSciences is committed to convenient, efficient, and cost-effective C. elegans model customization. Tell us your target design — knockout, knockin, tagging, or point mutation — and our scientists will respond with a tailored plan and quote.
Contact UsReferences
1. Kim H. M., Colaiácovo M. P. CRISPR-Cas9-guided genome engineering in C. elegans. Current Protocols in Molecular Biology, 2016, 115(1): 31.7.1–31.7.18.
2. Quazi F., Molday R. S. Differential phospholipid substrates and directional transport by ATP-binding cassette proteins ABCA1, ABCA7, and ABCA4. J Biol Chem, 2013, 288(48): 34414-34426.
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