H4417
Human Collagen Type IV
from human placenta, liquid, High Performance
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
Form:
solution
Biological source:
human placenta
Product Name
Collagen from human placenta, Bornstein and Traub Type IV, solution, suitable for cell culture, High Performance
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
Quality Level
Gene Information
human ... COL4A1(1282), COL4A2(1284), COL4A3(1285), COL4A4(1286), COL4A5(1287), COL4A6(1288)
Looking for similar products? Visit Product Comparison Guide
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.
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.
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
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.
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.
Disclaimer
Store this product at -20°C. It will retain activity for 2 years under these conditions.
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
高风险级别生物产品--人源产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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)
Tim Lämmermann et al.
Nature, 498(7454), 371-375 (2013-05-28)
Neutrophil recruitment from blood to extravascular sites of sterile or infectious tissue damage is a hallmark of early innate immune responses, and the molecular events leading to cell exit from the bloodstream have been well defined. Once outside the vessel
High fluence iontophoretic corneal collagen cross-linking: in vivo OCT imaging of riboflavin penetration.
Paolo Vinciguerra et al.
Journal of refractive surgery (Thorofare, N.J. : 1995), 29(6), 376-377 (2013-06-07)
Related Content
Instructions
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service