As indicated above under 'PROPERTIES', this collagen solution is sterile-filtered.
C2249
Human Collagen Type I
Collagen Solution from human fibroblasts
from human fibroblasts, liquid, 3 mg/mL, suitable for cell culture
Sinónimos:
Collagen Solution, Fibroblast Collagen
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About This Item
Código UNSPSC:
12352202
NACRES:
NA.75
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Nombre del producto
Collagen Solution from human fibroblasts, 3 mg/mL, sterile-filtered, BioReagent, suitable for cell culture
origen biológico
human fibroblasts
Nivel de calidad
esterilidad
sterile-filtered
Línea del producto
BioReagent
Formulario
solution
envase
pkg of 20 mL
concentración
3 mg/mL
técnicas
cell culture | mammalian: suitable
cobertura de la superficie
6‑10 μg/cm2
Especificidad de unión
Peptide Source: Collagen
Peptide Source: Elastin
actividad extraña
endotoxin ≤5.0 μmole/min-mg protein
Condiciones de envío
wet ice
temp. de almacenamiento
2-8°C
Descripción general
Collagen constitutes to one-third of the total protein in humans.[1] Collagen fibril is the basic component of the tissues containing collagen. It is predominantly expressed in the extracellular matrix.[1]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.
Aplicación
Acciones bioquímicas o fisiológicas
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.[5][6] 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.[7]
Proteins belonging to the collagen family supports and nourishes body tissues such as tendons, cartilage, skin and sclera of the eye.[8] Collagen type 1 is a versatile building material required for tissue elasticity and maintains its stability and strength.[9] Collagen is also present in byssus thread of invertebrates, which helps in surface attachment.[9] Defective collagen affects the biomechanical property of arterial tissues.[10]
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
nwg
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Los clientes también vieron
Cecilie Kjelgaard-Petersen et al.
Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals, 20(8), 547-556 (2016-02-11)
Characterize biomarkers measuring extracellular matrix turnover of inflamed osteoarthritis synovium. Human primary fibroblast-like synoviocytes and synovial membrane explants (SMEs) treated with various cytokines and growth factors were assessed by C1M, C3M, and acMMP3 in the conditioned medium. TNFα significantly increased
Collagen: structure and mechanics, an introduction
Collagen, 1-13 (2008)
Aspek Klinik, Genetik dan Molekuler Osteogensis Imperfekta
Mariska M and Auerkari EI
Journal of Dentistry Indonesia, 14(2), 95-110 (2015)
Frederick Grinnell
Trends in cell biology, 13(5), 264-269 (2003-05-14)
Research on fibroblast biology in three-dimensional collagen matrices offers new opportunities to understand the reciprocal and adaptive interactions that occur between cells and surrounding matrix in a tissue-like environment. Such interactions are integral to the regulation of connective tissue morphogenesis
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)
Artículos
Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.
Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.
Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.
Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.
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How did you steralize this collagen?
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Is this product suitable for 3D gel formation? How should it be neutralized? How quickly does it polymerize once neutralized? Is there a protocol available for 3D gel formation?
1 answer-
Procedure for 3-D Gel Preparation:
1. Mix 8 parts of chilled collagen solution with 1 part of
10 X PBS (Catalog Number P5493 or P5368) or
10 X culture medium. Cells may be added following
this step.2. Adjust pH of mixture prepared in step 1 to 7.2–7.6.
Use of 0.1 M NaOH (10-fold dilution of Catalog
Number S2770) or 0.01 M HCl (100-fold dilution of
Catalog Number H9892) is recommended. Monitor
pH adjustment carefully with pH meter, phenol red,
or pH paper.3. To prevent gelation, maintain temperature of the
mixture at 2–8C. To form gel, warm to 37C. For
best results allow 45 minutes to 1 hour for gel
formation.4. The gels can be dried under a laminar flow hood.
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What solvent is used for product C2249?
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The solvent for product C2249 is 13 mM HCl.
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What is the 2D Hydrogel protocol for Product No. C2249?
1 answer-
There has been no internal protocol for C2249 however this paper describes protocol for 2D Collagen Gel. Hong H, Stegemann JP. 2D and 3D collagen and fibrin biopolymers promote specific ECM and integrin gene expression by vascular smooth muscle cells. J Biomater Sci Polym Ed. 2008;19(10):1279-93. doi: 10.1163/156856208786052380. PMID: 18854122; PMCID: PMC2731795.
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Is this a monomer?
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This product is a mix of monomers, dimers, trimers, and oligomers, with some remaining collagen fragments.
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Is the monomer a tropocollagen?
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The human collagen is secreted from fibroblast cells, which cleave the loose ends of the procollagen molecule, leaving what is considered tropocollagen with the telopeptide region intact. An enzyme step is utilized to cleave the telopeptide, resulting in Atelocollagen, which maintains its triple helical formation but without the telopeptide region.
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What is the acid, and concentration of acid, that the collagen is solubilized within?
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The acid used to prepare this product is HCl. The final concentration of the solvent is 13 mM.
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