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Key Documents

C2249

Sigma-Aldrich

Human Collagen Type I

from human fibroblasts, liquid, 3 mg/mL, suitable for cell culture

Synonyme(s) :

Collagen Solution, Fibroblast Collagen

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About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.75

product name

Collagen Solution from human fibroblasts, 3 mg/mL, sterile-filtered, BioReagent, suitable for cell culture

Source biologique

human fibroblasts

Niveau de qualité

Stérilité

sterile-filtered

Gamme de produits

BioReagent

Forme

solution

Conditionnement

pkg of 20 mL

Concentration

3 mg/mL

Technique(s)

cell culture | mammalian: suitable

Couverture de surface

6‑10 μg/cm2

Spécificité de la liaison

Peptide Source: Collagen

Peptide Source: Elastin

Activité étrangère

endotoxin ≤5.0 μmole/min-mg protein

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Description générale

Collagen constitutes to one-third of the total protein in humans. Collagen fibril is the basic component of the tissues containing collagen. It is predominantly expressed in the extracellular matrix.Type I collagen is a major structural component of skin, bone, tendon, and other fibrous connective tissues. It differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. Type I collagen is a heterotrimer composed of two α1(I) chains and one alpha2(I) chain, which spontaneously form a triple helix scaffold at neutral pH and 37 °C. Purified human collagen solution is produced from neo-natal human fibroblasts that have secreted human extracellular matrix (hECM) using a propriety cell culture production system. This product contains a high monomer content. In vitro cultures were prepared using intensively tested human fibroblast cells and purified using a manufacturing process following applicable aspects of cGMP. The human fibroblast cells have undergone significant testing demonstrating safety from viruses and other adventitious agents. This process contains built-in, validated steps to ensure the inactivation of possible prion and/or viral contaminants.

Application

Collagen Solution from human fibroblasts has been used

  • as a component of coating solution for human bone marrow chip fabrication.
  • in fibroblast-like synoviocytes culturing.
  • as a coating solution for microchannels for organ chip culture

Actions biochimiques/physiologiques

Collagen is an essential ingredient of connective tissue. Studies in a Chinese family show that mutation in COL1A1 (collagenase type I) is linked with type I osteogenesis imperfecta. Collagen is linked with subchondral turnover of bone, and might have potential as marker to determine the state of joint space narrowing and osteophytes in osteoarthritis.
Proteins belonging to the collagen family supports and nourishes body tissues such as tendons, cartilage, skin and sclera of the eye. Collagen type 1 is a versatile building material required for tissue elasticity and maintains its stability and strength. Collagen is also present in byssus thread of invertebrates, which helps in surface attachment. Defective collagen affects the biomechanical property of arterial tissues.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Aspek Klinik, Genetik dan Molekuler Osteogensis Imperfekta
Mariska M and Auerkari EI
Journal of Dentistry Indonesia, 14(2), 95-110 (2015)
Collagen: structure and mechanics, an introduction
Collagen, 1-13 (2008)
Synovitis biomarkers: ex vivo characterization of three biomarkers for identification of inflammatory osteoarthritis
Kjelgaard PC, et al.
Biomarkers, 20(8), 547-556 (2015)
On-chip recapitulation of clinical bone-marrow toxicities and patient-specific pathophysiology
Chou DB, et al.
Nature Biomedical Engineering, 4(4), 394?406-394?406 (2020)
Collagen in arterial walls: biomechanical aspects
Collagen, 285-324 (2008)

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