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    recombinant-human-collagen-i-protein-ab158152.pdf

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Signal Transduction Cytoskeleton / ECM Extracellular Matrix ECM Proteins Collagen
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Recombinant Human Collagen I protein (ab158152)

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SDS-PAGE - Recombinant Human Collagen I protein (ab158152)

    Key features and details

    • Expression system: Wheat germ
    • Tags: GST tag N-Terminus
    • Suitable for: SDS-PAGE, WB, ELISA

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    Description

    • Product name

      Recombinant Human Collagen I protein
      See all Collagen I proteins and peptides
    • Expression system

      Wheat germ
    • Accession

      1277
    • Protein length

      Protein fragment
    • Animal free

      No
    • Nature

      Recombinant
      • Species

        Human
      • Sequence

        EGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETG PAGPAGPVGPVGARGPAGPQGPRGDKGETGEQGDRGIK
      • Predicted molecular weight

        35 kDa including tags
      • Amino acids

        1021 to 1108
      • Tags

        GST tag N-Terminus

    Associated products

    • Corresponding Antibody

      • Anti-Collagen I antibody [3G3] - BSA and Azide free (ab88147)

    Specifications

    Our Abpromise guarantee covers the use of ab158152 in the following tested applications.

    The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

    • Applications

      SDS-PAGE

      Western blot

      ELISA

    • Form

      Liquid
    • Additional notes

       

       

    • Concentration information loading...

    Preparation and Storage

    • Stability and Storage

      Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

      pH: 8.00
      Constituents: 0.31% Glutathione, 0.79% Tris HCl

    General Info

    • Alternative names

      • Alpha 1 type I collagen
      • Alpha 2 type I collagen
      • alpha 2 type I procollagen
      • alpha 2(I) procollagen
      • alpha 2(I)-collagen
      • Alpha-1 type I collagen
      • alpha1(I) procollagen
      • CO1A1_HUMAN
      • COL1A1
      • COL1A2
      • collagen 1
      • collagen alpha 1 chain type I
      • Collagen alpha-1(I) chain
      • collagen alpha-1(I) chain preproprotein
      • Collagen I alpha 1 polypeptide
      • Collagen I alpha 2 polypeptide
      • collagen of skin, tendon and bone, alpha-1 chain
      • collagen of skin, tendon and bone, alpha-2 chain
      • Collagen type I alpha 1
      • Collagen type I alpha 2
      • EDSC
      • OI1
      • OI2
      • OI3
      • OI4
      • pro-alpha-1 collagen type 1
      • type I proalpha 1
      • Type I procollagen
      • type I procollagen alpha 1 chain
      see all
    • Function

      Type I collagen is a member of group I collagen (fibrillar forming collagen).
    • Tissue specificity

      Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
    • Involvement in disease

      Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:114000]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.
      Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:130000]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.
      Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:130060]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.
      Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:166200]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.
      Defects in COL1A1 are a cause of osteogenesis imperfecta type 2A (OI2A) [MIM:166210]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency.
      Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:259420]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta.
      Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:166220]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta.
      Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:166710]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.
      Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.
    • Sequence similarities

      Belongs to the fibrillar collagen family.
      Contains 1 fibrillar collagen NC1 domain.
      Contains 1 VWFC domain.
    • Post-translational
      modifications

      Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some of the chains.
      O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.
    • Cellular localization

      Secreted > extracellular space > extracellular matrix.
    • Target information above from: UniProt accession P02452 The UniProt Consortium
      The Universal Protein Resource (UniProt) in 2010
      Nucleic Acids Res. 38:D142-D148 (2010) .

      Information by UniProt

    Images

    • SDS-PAGE - Recombinant Human Collagen I protein (ab158152)
      SDS-PAGE - Recombinant Human Collagen I protein (ab158152)
      ab158152 on a 12.5% SDS-PAGE stained with Coomassie Blue.

    Protocols

    To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.

    Click here to view the general protocols

    Datasheets and documents

    • Datasheet download

      Download

    References (0)

    Publishing research using ab158152? Please let us know so that we can cite the reference in this datasheet.

    ab158152 has not yet been referenced specifically in any publications.

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