{"product_id":"recombinant-escherichia-coli-colicin-e1-cea-bhp10505954","title":"Recombinant Escherichia coli Colicin-E1 (cea)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003ecea\u003c\/strong\u003e (also reported as cea; Colicin-E1) from Escherichia coli. In the supplied product notes, the target is described as \u003cem\u003eThis colicin is a channel-forming colicin.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e cea (also reported as cea; Colicin-E1). When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 1-522aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e in vitro E.coli expression system. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 64.3 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003ecea has been annotated as This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.; FUNCTION. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches. Ion channels often regulate membrane excitability and ionic homeostasis; observed changes in abundance or binding can reflect altered gating states, subunit composition, or compartment-specific trafficking.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: cea — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=cea\n- NCBI Gene search: cea — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=cea\n- Ensembl search: cea — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=cea\n- AlphaFold DB search: cea — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/cea\n- RCSB PDB search: cea — RCSB PDB — https:\/\/www.rcsb.org\/search?query=cea\n- PubMed search: cea transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=cea+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"100 ug","offer_id":53207322755437,"sku":"CSB-CF360926ENL-100UG","price":2700.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320588820845,"sku":"CSB-CF360926ENL-20UG","price":1620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF360926ENL-SDS.jpg?v=1778623121","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-escherichia-coli-colicin-e1-cea-bhp10505954","provider":"BioHippo","version":"1.0","type":"link"}