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Human Collagen Type V

Name: Human Collagen Type V
Brand: MM

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

Synonym(s):

Collagen Type V

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About This Item

UNSPSC Code:

12352202

eCl@ss:

32160405

NACRES:

NA.75

product name

Human Collagen Type V,

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)

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Attachment Factors

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.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

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Collagens--structure, function, and biosynthesis.

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

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)

Beneficial regulation of fibrillar collagens, heat shock protein-47, elastin fiber components, transforming growth factor-β1, vascular endothelial growth factor and oxidative stress effects by copper in dermal fibroblasts.

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

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)

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Protocols

ECM Coating Protocols for Millicell®

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

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