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Your Position: Home > Protein > KREMEN2 > KR2-H52H3

Human Kremen-2 protein, His Tag

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  • Synonym
    KREMEN2, Kremen-2, KRM2, Dickkopf receptor 2,Kringle domain-containing transmembrane protein 2
  • Source
    Human Kremen-2, His Tag(KR2-H52H3) is expressed from human 293 cells (HEK293). It contains AA Gly 26 - Ala 364 (Accession # Q8NCW0-1).
  • Molecular Characterization
    KREMEN2 Structure

    This protein carries a polyhistidine tag at the C-terminus.

    The protein has a calculated MW of 38.0 kDa. The protein migrates as 45-60 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method / rFC method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, 0.2 M Arginine, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
KREMEN2 SDS-PAGE

Human Kremen-2, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

Bioactivity-ELISA
 KREMEN2 ELISA

Immobilized Human Dkk-1, Fc Tag (Cat. No. DK1-H5258) at 2 μg/mL (100 μL/well) can bind Human Kremen-2, His Tag (Cat. No. KR2-H52H3) with a linear range of 5-78 ng/mL (QC tested).

  • Background
    Kremen2 (Krm2) plays an important role in embryonic development, bone formation, and tumorigenesis as a crucial regulator of classical Wnt/β-catenin signaling pathway. Krm1 and its paralog Krm2 share the ability to bind Dkk1 and inhibit Wnt signaling, both processes previously shown to rely on the extracellular domain. Previous studies have shown that Krm2 may be involved in embryonic development, bone formation, neural ridge formation and tumorigenesis and could be a biomarker of grading and a potential therapeutic target in gastric cancer.
  • Clinical and Translational Updates

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