Overview

Description

  • Nature

    Native
  • Source

    Native
  • Amino Acid Sequence
    • Accession
    • Species

      Human

Specifications

Our Abpromise guarantee covers the use of ab134516 in the following tested applications.

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

  • Applications

    ELISA

    SDS-PAGE

  • Form

    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

  • Reconstitution
    Solubilize the white, hygroscopic powder slowly in 10 mM acetic acid (0.2% w/v) and adjust to neutral pH by adding 2/5 vol. 2.5X Carbonate buffer (0.25 M NaHCO3, 1.25 M NaCl, 0.1% NaN3).

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 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.
  • Information by UniProt

Images

  • SDS PAGE analysis of ab134516.

References

ab134516 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

Answer

Thank you for contacting us and your interest in our products.

We have a number of collagen I protein products in our catalogue. The collagen protein ab7526 is purified from the full length native bovine protein by a process involving limited pepsin digestion. The exact purity for this product is not determined.


We do however have a number of other products available. The Collagen I protein ab64010 which has been purified from bovine placental villi using controlled and limited pepsin digestion, followed by selective salt precipitation. This has estimated to be 90% pure by SDS page.

Alternatively, the ab134516 is purified from Human tendon using Guanidin-HCl extraction, pepsin digestion, salt precipitation, ion exchange chromatography and gel filtration. The sample should be mostly collagen I as "In healthy adult tendons, 95% of the collagen is type I” and “the remaining 5% constitutes small amounts of collagen types III, V, VI, XII and XIV”, (Excerpt from „Achilles Tendon Pathology”, Author: Richard Hargrove, MBBS, FRCS(Ire) (2005) and Riley GP: Gene expression and matrix turnover in overused and damaged tendons. Scandinavian journal of medicine & science in sports 2005, 15(4):241-251.)”).

The SDS PAGE gel performed using this protein can be observed on the datasheet of ab134516.

I hope this information has been of some help. If you have any further questions, please do not hesitate to contact us.

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