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Sigma-Aldrich

Bovine Collagen Type I

from bovine skin, liquid, 6 mg/mL, suitable for cell culture, used for 3D gel formation

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About This Item

Numer MDL:
MFCD00130825
Kod UNSPSC:
12352202
NACRES:
NA.75

product name

Collagen solution from bovine skin, Type I, 6 mg/mL, sterile-filtered, BioReagent, and for 3D matrix formation., suitable for cell culture

pochodzenie biologiczne

bovine skin

Poziom jakości

200

sterylność

sterile-filtered

linia produktu

BioReagent

Postać

liquid

opakowanie

pkg of 50 mL

stężenie

6 mg/mL

metody

cell culture | mammalian: suitable using and for 3D matrix formation.

pokrycie powierzchni

6‑10 μg/cm2

Specyficzność wiązania

Peptide Source: Collagen

Peptide Source: Elastin

Peptide Source: Fibronectin

obecność zanieczyszczeń

endotoxin ≤1.0 μmole/min-mg protein

Warunki transportu

wet ice

temp. przechowywania

2-8°C

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Opis ogólny

In mammals, collagen type 1 is a widely expressed fibrous protein. It 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, and is also found in arterial walls, tendons, ligaments, skin, cornea, bone and dentin. Collagen structure possesses a triple helix polypeptide strand.

Zastosowanie

Collagen solution from bovine skin has been used as a substrate in cell adhesion assay.
This highly purified solution is suitable for 3-D matrix formation in cell culture. 3-D collagen gels imitate the in vivo cell physiology better than traditional 2D systems and has been proven successful for several cell types including cardian and corneal fibroblasts, depatic stellate cells, and neuroblastoma cells. Such 3-D gels are also useful in studies of mechanotransduction, cell signaling involving the transformation of mechanical signals into biochemical signals

Działania biochem./fizjol.

Collagen type 1 is a versatile building material required for tissue elasticity and maintains the stability and strength in a variety of tissues. Collagen is also present in byssus thread of invertebrates, which helps in surface attachment. Defective collagen affects the biomechanical property of arterial tissue.
In 3D environments, cell extensions can use integrins on cell surfaces to activate specific signaling pathways and integran-independent mechanical interactions resulting from the entanglement of matrix fibrils is possible.

Komponenty

Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. As a heterodimer composed of two a1 chains and one a2 chains, it spontaneously forms a triple helix scaffold at neutral pH and 37°C.

Uwaga dotycząca przygotowania

This product is prepared from type I bovine collagen purified and extracted from skin and contains a high monomer content. The raw collagen used to prepare this product has been isolated from a closed herd and purified with a GMP manufacturing process that includes inactivation of any possible prion or viral contamination. As supplied, it is a 6 mg/mL aqueous solution in 0.01 M HCl at a pH of 2.0.

Inne uwagi

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Be wary of confusing Sigma-type designations with recognized collagen classification types.
This page may contain text that has been machine translated.

Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

nwg

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Collagen: structure and mechanics, an introduction
Collagen, 1-13 (2008)
Collagen in arterial walls: biomechanical aspects
Collagen, 285-324 (2008)
Sanghun Park et al.
Biomolecules, 12(6) (2022-06-25)
Among future food problems, the demand for meat is expected to increase rapidly, but the production efficiency of meat, which is a protein source, is very low compared to other foods. To address this problem, research on the development and
Dario Mendes Júnior et al.
Antibiotics (Basel, Switzerland), 10(6) (2021-07-03)
The experimental use of poly (alcohol-vinyl) (PVA) as a skin curative is increasing widely. However, the use of this hydrogel is challenging due to its favorable properties for microbiota growth. The association with silver nanoparticles (AgNPs) as an antimicrobial agent
Richard G J Dohmen et al.
NPJ science of food, 6(1), 6-6 (2022-01-26)
Cultured meat is an emergent technology with the potential for significant environmental and animal welfare benefits. Accurate mimicry of traditional meat requires fat tissue; a key contributor to both the flavour and texture of meat. Here, we show that fibro-adipogenic
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