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Sigma-Aldrich

Human Collagen Type V

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About This Item

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

biological source

human

Quality Level

100

assay

95% (SDS-PAGE)

form

liquid

manufacturer/tradename

Chemicon®

concentration

1 mg/mL

technique(s)

cell culture | mammalian: suitable

impurities

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

input

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)

NCBI accession no.

NM_000093.3

UniProt accession no.

P20908

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... COL5A1(1289) , COL5A2(1290)

Related Categories

General description

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.

Application

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.

Biochem/physiol Actions

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.

Physical form

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

Preparation Note

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

Storage and Stability

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

Other Notes

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.

Legal Information

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

Disclaimer

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.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘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
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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