{"product_id":"recombinant-arabidopsis-thaliana-protein-hapless-2-hap2-bhp10514998","title":"Recombinant Arabidopsis thaliana Protein HAPLESS 2 (HAP2)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eHAP2\u003c\/strong\u003e (also reported as GENERATIVE CELL SPECIFIC 1) from Arabidopsis thaliana (Mouse-ear cress). In the supplied product notes, the target is described as \u003cem\u003eRequired for male fertility.\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 HAP2 (also reported as GENERATIVE CELL SPECIFIC 1). 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 25-705aa. 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 E.coli. 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: 82.3 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\u003eHAP2 is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. 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.\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\u003eDomain-resolved biology: extracellular\/luminal domains and cytosolic tails are being dissected to understand modular functions such as ligand binding, scaffolding, and post-translational regulation.\u003c\/li\u003e\n  \u003cli\u003eProteomics and interactomics: proximity labeling and quantitative proteomics continue to expand maps of membrane protein complexes and trafficking determinants.\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: HAP2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=HAP2\n- NCBI Gene search: HAP2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=HAP2\n- Ensembl search: HAP2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=HAP2\n- AlphaFold DB search: HAP2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/HAP2\n- RCSB PDB search: HAP2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=HAP2\n- PubMed search: HAP2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=HAP2+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":"1 mg","offer_id":53207340613997,"sku":"CSB-EP518991DOA(A4)-1MG","price":2466.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320613790061,"sku":"CSB-EP518991DOA(A4)-100UG","price":729.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320613822829,"sku":"CSB-EP518991DOA(A4)-20UG","price":388.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP518991DOA_A4_-SDS.jpg?v=1778623173","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-arabidopsis-thaliana-protein-hapless-2-hap2-bhp10514998","provider":"BioHippo","version":"1.0","type":"link"}