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Human Collagen Type V

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

Sinônimo(s):

Collagen Type V

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About This Item

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

product name

Human Collagen Type V,

fonte biológica

human

Nível de qualidade

Ensaio

95% (SDS-PAGE)

forma

liquid

fabricante/nome comercial

Chemicon®

concentração

1 mg/mL

técnica(s)

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 adesão NCBI

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

Informações sobre genes

Descrição geral

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

Aplicação

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). It has also been used to incubate the 96 well plate to determine the protein levels in media and cell lysates of fibroblasts.

Ações bioquímicas/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.

forma física

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

Nota de preparo

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

Armazenamento e estabilidade

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

Outras 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.

Informações legais

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

Exoneração de responsabilidade

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 classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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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
Characterization of a novel collagen chain in human placenta and its relation to AB collagen.
Sage, H and Bornstein, P
Biochemistry, 18, 3815-3822 (1979)
R W Glanville et al.
European journal of biochemistry, 95(2), 383-389 (1979-04-02)
Native type IV collagen was isolated from human placenta using pepsin solubilisation followed by fractional salt precipitation and chromatogarphic purification. The native preparation was characterised using amino acid analyses, disc gel electrophoresis, segment-long-spacing crystallites and immunological methods. Two component alpha

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