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Your Position: Home > Protein > Pro-COL1A1 > PC1-M5243

Mouse Pro-COL1A1 Protein, His Tag, low endotoxin (MALS verified)

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  • Source
    Mouse Pro-COL1A1 Protein, His Tag(PC1-M5243) is expressed from human 293 cells (HEK293). It contains AA Gln 23 - Ser 151 (Accession # P11087).
  • Molecular Characterization
    Pro-COL1A1 Structure

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

    The protein has a calculated MW of 15.9 kDa. The protein migrates as 25-27 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 0.01 EU per μg by the LAL method.
  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5 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
Pro-COL1A1 SDS-PAGE

Mouse Pro-COL1A1 Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS
Pro-COL1A1 MALS images

The purity of Mouse Pro-COL1A1 Protein, His Tag (Cat. No. PC1-M5243) is more than 85% and the molecular weight of this protein is around 15-25 kDa verified by SEC-MALS.

  • Background
    Type I collagen is the most abundant structural protein of connective tissues such as skin, bone and tendon. It is synthesized as a procollagen molecule which is characterized by a 300 nm triple helical domain flanked by globular N- and C-terminal propeptides. The triple helical domain contains Gly-Xaa-Yaa triplets where Xaa and Yaa are frequently proline and hydroxyproline, respectively. The non-helical propeptides are removed by procollagen N- and C-proteinase activities so that the mature triple helices can self-assemble into collagen fibrils that provide tensile strength to tissues. Type I collagen is a heterotrimer that consists of two alpha 1(I) chains and one alpha 2(I) chain, although homotrimers consisting of three identical alpha 1(I) chains have also been described .
  • Clinical and Translational Updates

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ETA of in-stock products: 2 business days

Price(USD) : $350.00

Price(USD) : $2310.00

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