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Human Claudin-3 Full Length Protein, His,Twin-Strep Tag (Detergent)

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Cat. No. / Size
Price
Qty
CL3-H5583-20ug
$805.00
CL3-H5583-100ug
$2985.00
CL3-H5583-500ug
$7480.00
ETA of in-stock products:2 business days
Sub-Total$ 0

Product Details

  • Application

    1. Immunization
    2. Affinity testing (SPR / BLI)
    3. Screening (ELISA)
  • Synonyms

    C7orf1, CPE-R2, CPETR2, HRVP1, RVP1

  • Source

    Detergent Human Claudin-3 Full Length Protein, His,Twin-Strep Tag (CL3-H5583) is expressed from Baculovirus-Insect cells. It contains AA Met 1 - Val 220 (Accession # NP_001297.1).

    Predicted N-terminus: Met

    Request for sequence
  • Molecular Characterization

    Claudin-3 Structure

    Other Tags and Version Biotin & Other Labeled Version

    This protein carries a polyhistidine tag at the N-terminus and a twin strep tag at the C-terminus.

    The protein has a calculated MW of 28.7 kDa. The protein migrates as 27-28 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

    *The detergent Buffer B (Cat. No. LG-13) is sold separately and not included in protein, you can follow the link for product information.

    1. Structure

      Each full-length transmembrane protein is encapsulated by detergent micelle.

    2. Synthesis Process

      Through mild detergent micelle extraction, dedicated solubilization, and stringent affinity purification, we maximally retain the native transmembrane conformation of full-length transmembrane proteins throughout downstream purification. This workflow yields purified, detergent-solubilized proteins free of unrelated membrane impurities and exogenous scaffold proteins, with exceptional purity, accurate quantitation, and well-preserved biological activity—ideal for immunization, binding assays in antibody discovery and screening (ELISA) and affinity testing (SPR and BLI), etc.

  • Purity

    >85% as determined by SDS-PAGE.

  • Formulation

    This product is not suitable for cell based experiments due to cytotoxicity of detergent.
    Detergent buffer is INDISPENSABLE to keep membrane protein soluble and active, under no circumstances should you remove detergent.
    Detergent buffer is sold separately and not included in protein, and please contact us if you need the buffer.
    If glycerol is not compatible with your application, remove glycerol just before the immediate experiment, and NEVER store glycerol-free protein solution.

    Supplied as 0.2 μm filtered solution in 50 mM HEPES, 150 mM NaCl, Buffer B, pH7.5 with glycerol as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 3 months under sterile conditions.
  • ACRO Quality Management System

    1. QMS(ISO, GMP)
    2. Quality Advantages
    3. Quality Control Process

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Performance Data

  • SDS-PAGE

    Claudin-3 SDS-PAGE

    Human Claudin-3 Full Length Protein, His,Twin-Strep Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 85% (With Star Ribbon Pre-stained Protein Marker).

  • Bioactivity-ELISA

     Claudin-3 ELISA

    Immobilized Human Claudin-3 Full Length Protein, His,Twin-Strep Tag (Cat. No. CL3-H5583) at 5 μg/mL (100 μL/well) on a Nickel Coated plate (Cat. No. SP-19) can bind Anti-Claudin 3 Antibody with a linear range of 0.2-13 ng/mL (QC tested).

    Protocol
  • Bioactivity-SPR

     Claudin-3 SPR

    Anti-Claudin 3 Antibody captured on Protein A Chip can bind Human Claudin-3 Full Length Protein, His,Twin-Strep Tag (Cat. No. CL3-H5583) with an affinity constant of 161 nM as determined in a SPR assay (in presence of LG-13) (Biacore 8K) (Routinely tested).

    Protocol

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Background

A high-affinity receptor for Clostridium perfringens enterotoxin (CPE) and a core component of tight junctions. Claudin-3 is robustly overexpressed in breast, ovarian, and prostate cancers. This makes it a leading target for CPE-based therapeutic toxins designed to selectively lyse malignant epithelial cells.

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