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C5608

Sigma-Aldrich

Collagen from rabbit skin

Bornstein and Traub Type I, powder

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100 MG
$559.000

$559.000


Fecha estimada de envío21 de abril de 2025


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100 MG
$559.000

About This Item

Número de CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.61

$559.000


Fecha estimada de envío21 de abril de 2025


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origen biológico

rabbit skin

Nivel de calidad

descripción

acid soluble

Formulario

powder

técnicas

cell culture | stem cell: suitable

solubilidad

aqueous acid: ≤10 mg/mL
aqueous sodium acetate buffer: soluble (0.01-0.5M)

Nº de acceso UniProt

temp. de almacenamiento

2-8°C

Información sobre el gen

Descripción general

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Do not confuse Sigma type designations with recognized collagen classification types.

Aplicación

Collagen-type 1 may be used in research of Idiopathic pulmonary fibrosis (IPF). Robust expression of collagen-type 1 is one distinctive feature of IPF. Additionally, collagen-type 1 has been used in studies on the effect of endoplasmic reticulum (ER) stress from IPF on myofibroblastic differentiation of lung fibroblasts. Collage-type 1 soluble in acidic solution produces three dimensional scaffolding useful in bioengineering and cell culture applications where biomaterials are needed to replace native collagen extracellular matrices.

Collagen Type I has been used as a scaffold for the growth in vitro of stem cells in a wide variety of biomaterial engineering studies.

Nota de preparación

Prepared with modification of Gallop, P.M.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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The Journal of cell biology, 201(7), 1069-1084 (2013-06-27)
Cell migration through 3D tissue depends on a physicochemical balance between cell deformability and physical tissue constraints. Migration rates are further governed by the capacity to degrade ECM by proteolytic enzymes, particularly matrix metalloproteinases (MMPs), and integrin- and actomyosin-mediated mechanocoupling.

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