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CC077

Sigma-Aldrich

Human Collagen Type V

from human placenta, liquid, 1 mg/mL, suitable for cell culture, used for gel formation

Sinónimos:

Collagen Type V

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100 μG
516,00 €

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100 μG
516,00 €

About This Item

Código UNSPSC:
12352202
eCl@ss:
32160405
NACRES:
NA.75

516,00 €


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Nombre del producto

Human Collagen Type V,

origen biológico

human

Nivel de calidad

Ensayo

95% (SDS-PAGE)

Formulario

liquid

fabricante / nombre comercial

Chemicon®

concentración

1 mg/mL

técnicas

cell culture | mammalian: suitable

impurezas

<0.5% non-collagen proteins
<1% collagen type III
<2% collagen type I
<2% collagen type IV

entrada

sample type mesenchymal stem cell(s)
sample type induced pluripotent stem cell(s)
sample type pancreatic stem cell(s)
sample type epithelial cells
sample type neural stem cell(s)
sample type hematopoietic stem cell(s)
sample type: human embryonic stem cell(s)

Nº de acceso NCBI

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

Información sobre el gen

Descripción general

Collagen type V is fibril-forming collagen that is located in the lung, bone, and fetal membranes along with type I collagen.[1] It is minor collagen present in the extracellular matrix.[2]

Aplicación

Human Collagen Type V has been used to study the interaction of high endothelial venule protein (hevin) with human collagen V by fluorescence polarization (FP) assay and surface plasmon resonance(SPR).[3] It has also been used to incubate the 96 well plate to determine the protein levels in media and cell lysates of fibroblasts.[1]

Acciones bioquímicas o fisiológicas

Collagen type V acts as a regulator of collagen fibrillogenesis in the cornea and skin dermis. It interacts with matrix collagens and structural proteins thereby contributing to the structural integrity of tissues. Lower levels of type V collagen lead to loss of corneal transparency and Ehler Danlos syndrome.[2]

Forma física

Liquid, in 0.1M acetic acid, pH 3.0. No preservatives added.

Nota de preparación

Purified by serial salt precipitations of a pepsin extraction of human fetal membranes and chromatography on DEAE-cellulose.

Almacenamiento y estabilidad

Maintain at -20°C in undiluted aliquots for up to 12 months. Do not thaw and refreeze.

Otras notas

Molecular composition: α1(V)]2 α2(V), native triple helix. Purity and retention of the native helical structure were monitored by SDS-PAGE, ORD measurement, and by reaction with anti-collagen type-specific monoclonal antibodies. Product Source: Human placenta, negative for HBsAg and HIV antibodies.

Información legal

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Cláusula de descargo de responsabilidad

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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The effects of tissue pretreatment and pepsin levels on the isolation of collagens from human placenta.
Klasson, S C, et al.
Collagen and Related Research, 6, 397-408 (1986)
Type V collagen in health, disease, and fibrosis
The Anatomical Record, 299(5), 613-629 (2016)
K Gelse et al.
Advanced drug delivery reviews, 55(12), 1531-1546 (2003-11-19)
The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified so far. Collagens are
Neena Philips et al.
Connective tissue research, 53(5), 373-378 (2012-02-14)
Skin aging is associated with the loss of the structural collagens and the elastin fiber components that form the extracellular matrix (ECM). It is associated with reduced transforming growth factor-β (TGF-β), angiogenesis and increased oxidative stress. Copper has been incorporated
Shanghua Fan et al.
Structure (London, England : 1993), 29(7), 664-678 (2021-02-04)
Hevin is secreted by astrocytes and its synaptogenic effects are antagonized by the related protein, SPARC. Hevin stabilizes neurexin-neuroligin transsynaptic bridges in vivo. A third protein, membrane-tethered MDGA, blocks these bridges. Here, we reveal the molecular underpinnings of a regulatory network

Protocolos

This page covers the ECM coating protocols developed for four types of ECMs on Millicell®-CM inserts, Collagen Type 1, Fibronectin, Laminin, and Matrigel.

Preguntas

Revisiones

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Filtros activos

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