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CC076

Sigma-Aldrich

Human Collagen Type IV

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About This Item

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

biological source

human

Quality Level

Assay

95% (Human collagen type IV, SDS-PAGE)

form

liquid

mol wt

300 kDa

manufacturer/tradename

Chemicon®

concentration

1 mg/mL

technique(s)

cell culture | mammalian: suitable

impurities

<5% Human collagen types I-III, V, VI, and non-collagen proteins

input

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

solubility

water: soluble at 20 °C

NCBI accession no.

UniProt accession no.

Binding Specificity

Peptide Source: Laminin

Peptide Source: Nidogen

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... COL4A1(1282)

Related Categories

General description

Collagen type IV is the major structural element of basal membranes. Human collagen type IV is a native triple helix. Collagen was extracted from washed dissected tissue into dilute acetic acid after mild pepsin treatment. The Collagen type IV was purified by using differential salt precipitation. Purity and retention of native helical structure was controlled by SDS-PAGE and by reaction with anti-collagen type specific monoclonal antibodies. Molecular weight: 300kDa; Solubility: 10mg/mL
Product Source: Human placenta, negative for HBsAg and HIV antibodies

Application

Coating material for cell culture studies

Formation of collagen gels

Optimal working dilutions must be determined by end user.

Physical form

Liquid purified protein. In 100 μL of 0.5M acetic acid solution, pH 2.5. Salt-free, no preservative.

Storage and Stability

Store at -20ºC for up to 12 months. Avoid repeated freeze/thaw cycles.

Analysis Note

Retention of native structure was confirmed by ability to form microfibrils.

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 Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain.
Bentz, H, et al.
Proceedings of the National Academy of Sciences of the USA, 80, 3168-3172 (1983)
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

Articles

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

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