As indicated above under 'PROPERTIES', this collagen solution is sterile-filtered.
C2249
Human Collagen Type I
from human fibroblasts, liquid, 3 mg/mL, suitable for cell culture
Collagen Solution from human fibroblasts
Sinónimos:
Collagen Solution, Fibroblast Collagen
Iniciar sesión para ver los precios por organización y contrato.
Seleccione un Tamaño
20 ML
$941.00
Acerca de este artículo
UNSPSC Code:
12352202
NACRES:
NA.75
Biological source:
human fibroblasts
Form:
solution
Technique(s):
cell culture | mammalian: suitable
Concentration:
3 mg/mL
Saltar a
Servicio técnico
¿Necesita ayuda? Nuestro equipo de científicos experimentados está aquí para ayudarle.
Permítanos ayudarleNombre del producto
Collagen Solution from human fibroblasts, 3 mg/mL, sterile-filtered, BioReagent, suitable for cell culture
biological source
human fibroblasts
sterility
sterile-filtered
product line
BioReagent
form
solution
packaging
pkg of 20 mL
concentration
3 mg/mL
technique(s)
cell culture | mammalian: suitable
surface coverage
6‑10 μg/cm2
binding specificity
Peptide Source: Collagen
, Peptide Source: Elastin
foreign activity
endotoxin ≤5.0 μmole/min-mg protein
shipped in
wet ice
storage temp.
2-8°C
Quality Level
¿Está buscando productos similares? Visita Guía de comparación de productos
1 of 4
Este artículo | |||
|---|---|---|---|
| sterility sterile-filtered | sterility sterile-filtered | sterility sterile-filtered | sterility sterile-filtered |
| technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable (and for 3D matrix formation) | technique(s) cell culture | mammalian: suitable using and for 3D matrix formation. | technique(s) cell culture | mammalian: suitable |
| biological source human fibroblasts | biological source bovine skin | biological source bovine skin | biological source human cell culture |
| concentration 3 mg/mL | concentration 2.9-3.2 mg/mL | concentration 6 mg/mL | concentration 0.3 mg/mL |
| Quality Level 100 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| form solution | form liquid | form liquid | form solution |
General description
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.
Application
Biochem/physiol Actions
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]
Clase de almacenamiento
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Elija entre una de las versiones más recientes:
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
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)
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)
Artículos
Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.
-
How did you steralize this collagen?
1 answer-
Helpful?
-
-
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.
Helpful?
-
-
Is the monomer a tropocollagen?
1 answer-
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.
Helpful?
-
-
What solvent is used for product C2249?
1 answer-
The solvent for product C2249 is 13 mM HCl.
Helpful?
-
-
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.
Helpful?
-
-
Is this a monomer?
1 answer-
This product is a mix of monomers, dimers, trimers, and oligomers, with some remaining collagen fragments.
Helpful?
-
-
What is the acid, and concentration of acid, that the collagen is solubilized within?
1 answer-
The acid used to prepare this product is HCl. The final concentration of the solvent is 13 mM.
Helpful?
-
Active Filters
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico