Merck
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H4417

Sigma-Aldrich

Collagen from human placenta

Bornstein and Traub Type IV, solution, suitable for cell culture, High Performance

CAS Number:
EC Number:
MDL number:
NACRES:
NA.51

Quality Level

biological source

human placenta

form

solution

technique(s)

cell culture | mammalian: suitable

surface coverage

<5 μg/cm2

impurities

Endotoxin, tested
HIV, hepatitis B and hepatitis C, none detected

storage temp.

−20°C

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Application

Type IV collagen has been found to play a key role in angiogenesis, neurological diseases and metastasis. Collagen from human placenta has been used to assess the bioelectric effects of quinine on airway epithelial cells, to study the selective toxicity of engineered lentvirus lytic peptides and in a particle aggregation assay for the rapid detection of fibronectin, fibrinogen and collagen receptors on Staphylococcus aureus. It has also been used in a magnesium-dependent, collagen-binding assay during characterization of human lung tumor-associated antigens.

Biochem/physiol Actions

During development, collagen IV is ubiquitously distributed in BMs. During the maturation process, this network gets partially replaced in a remarkably tissue specific manner, defining BM structure and function. Collagen IV has been shown to bind to platelets, hepatocytes, keratinocytes, endothelial, mesangial, pancreatic cells and some tumor cells.


Tissue injury in the autoimmune disease Goodpasture syndrome is due to pathogenic autoantibodies targeting the Collagen IV α3 chain . Mutations in COL4A5 are associated with Alport syndrome.

Components

All collagen molecules are composed of three polypeptide chains arranged in a triple helical conformation, with a primary structure that is mostly a repeating motif with glycine in every third position and proline or 4-hydroxyproline frequently preceding the glycine residue. Type IV collagen occurs only in the basement membranes and contains up to six genetically distinct a-chains.

Caution

Store this product at -20°C. It will retain activity for 2 years under these conditions.

Preparation Note

This product is supplied as a solution in 0.5 M acetic acid. It can be used to coat tissue-culture surfaces to promote cell attachment. The amount used in these applications is dependent on the cell type, plastic ware and incubation time. A recommended amount is 0.5-5 μg/cm2. It was prepared by pepsin extraction and chromatographic purification.

Other Notes

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Be wary of confusing Sigma-type designations with recognized collagen classification types.

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

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Certificate of Origin

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Quotes and Ordering

Akiko Nagaishi et al.
Nihon rinsho. Japanese journal of clinical medicine, 71(5), 876-880 (2013-06-20)
Patients with myasthenia gravis(MG) are divided into three groups: (1) acetylcholine receptor antibody positive MG: 80%, (2) muscle-specific receptor tyrosine kinase (MuSK) antibody positive MG: 5-10%, and (3) double seronegative MG. In 2011, autoantibodies (Abs) against low-density lipoprotein receptor-related protein
Katarina Wolf et al.
The Journal of cell biology, 201(7), 1069-1084 (2013-06-27)
Cell migration through 3D tissue depends on a physicochemical balance between cell deformability and physical tissue constraints. Migration rates are further governed by the capacity to degrade ECM by proteolytic enzymes, particularly matrix metalloproteinases (MMPs), and integrin- and actomyosin-mediated mechanocoupling.
Visian toric ICL implantation for residual refractive errors after ICRS implantation and corneal collagen cross-linking in keratoconus.
Elias Jarade et al.
Journal of refractive surgery (Thorofare, N.J. : 1995), 29(7), 444-444 (2013-07-04)
Simon Holland et al.
Current opinion in ophthalmology, 24(4), 302-309 (2013-05-18)
Topography-guided laser refractive surgery regularizes the front corneal surface irregularities to achieve the desired refractive outcome. This is particularly applicable in highly aberrated corneas, where wavefront aberrometry is often not possible. This article aims to review the recently published results
Michelle K Nguyen et al.
Current opinion in ophthalmology, 24(4), 291-295 (2013-06-06)
To describe the use of corneal collagen cross-linking (CXL) and its efficacy in the stabilization of keratorefractive procedures, including PRK, laser in-situ keratomileusis (LASIK), thermal keratoplasty, and orthokeratology. Since its introduction, CXL has quickly gained interest in the treatment of

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