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COL1A1 Protein (AA 1021-1109) (GST tag)

COL1A1 Origin: Human Host: Escherichia coli (E. coli) Recombinant > 95 % as determined by reducing SDS-PAGE.
Catalog No. ABIN7505044
  • Target See all COL1A1 Proteins
    COL1A1 (Collagen, Type I, alpha 1 (COL1A1))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1021-1109
    Origin
    • 10
    • 3
    • 3
    • 1
    Human
    Source
    • 14
    • 2
    • 1
    Escherichia coli (E. coli)
    Purification tag / Conjugate
    This COL1A1 protein is labelled with GST tag.
    Sequence
    Glu 1021-Gly 1109
    Characteristics
    A DNA sequence encoding the Human COL1A1 protein (P02452) (Glu1021-Gly1109) was expressed with a N terminal GST tag.
    Purity
    > 95 % as determined by reducing SDS-PAGE.
    Top Product
    Discover our top product COL1A1 Protein
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Buffer
    Lyophilized from sterile PBS, pH 7.4.
    Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
    Expiry Date
    12 months
  • Target
    COL1A1 (Collagen, Type I, alpha 1 (COL1A1))
    Alternative Name
    Collagen alpha-1 chain (COL1A1 Products)
    Background

    Abbreviation: Collagen alpha-1 chain,COL1A1

    Target Synonym: Collagen alpha-1(I) chain,Alpha-1 type I collagen,COL1A1,COL1A1

    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. This recombinant mini pro-alpha 1(I) collagen consists of a shortened alpha 1(I) chain with following domain structure from N- to C-terminus: N-propeptide, N?telopeptide, the 33 most N-terminal Gly-Xaa-Yaa repeats, the 33 most C-terminal Gly-Xaa-Yaa repeats, C-telopeptide and C-propeptide. The preparation contains a mixture of the full-length molecule, pN collagen I( alpha 1) and the C-terminal propeptide. This truncated pro-alpha 1(I) collagen is a substrate for procollagen N-proteinase and procollagen C-proteinase.

    Molecular Weight

    Calculated MW: 34.68 kDa

    Observed MW: 35 kDa

    UniProt
    P02452
    Pathways
    Sensory Perception of Sound, Autophagy, Growth Factor Binding
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