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Your Position: Home > Protein > AGR2 > AG2-M52H6

Mouse AGR2 / AG-2 Protein, His Tag (MALS verified)

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  • Synonym
    Anterior gradient protein 2 homolog,AG-2,hAG-2,HPC8,Secreted cement gland protein XAG-2 homolog,AGR2
  • Source
    Mouse AGR2, His Tag(AG2-M52H6) is expressed from human 293 cells (HEK293). It contains AA Lys 21 - Leu 175 (Accession # O88312-1).
    Predicted N-terminus: Lys 21
  • Molecular Characterization
    AGR2 Structure

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

    The protein has a calculated MW of 19.8 kDa. The protein migrates as 23 kDa and 24 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

    The protein is designed as a dimer.

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

    >95% as determined by SDS-PAGE.

    >90% as determined by SEC-MALS.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, 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
AGR2 SDS-PAGE

Mouse AGR2, 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%.

SEC-MALS
AGR2 MALS images

The purity of Mouse AGR2, His Tag (Cat. No. AG2-M52H6) is more than 90% and the molecular weight of this protein is around 55-68 kDa verified by SEC-MALS.

  • Background
    Anterior gradient 2 (AGR2) is a normal endoplasmic reticulum protein that has two important abnormal functions, amphibian limb regeneration and human cancer metastasis promotion. These normal intracellular and abnormal extracellular roles can be attributed to the multidomain structure of AGR2. The NMR structure shows that AGR2 consists of an unstructured N-terminal region followed by a thioredoxin fold.
  • Clinical and Translational Updates

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