C8374
Human Collagen Type IV
from human placenta, powder
Synonim(y):
Collagen from human placenta, Collagen Type 4
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Pozwól nam pomócNazwa produktu
Collagen from human placenta, Bornstein and Traub Type IV, powder
biological source
human placenta
assay
>85% (SDS-PAGE)
form
powder
technique(s)
cell culture | stem cell: suitable
impurities
HIV, hepatitis B and hepatitis C, none detected
solubility
0.5 M acetic acid: 1 mg/mL, clear to very slightly hazy
storage temp.
−20°C
Quality Level
Gene Information
human ... COL4A1(1282), COL4A2(1284), COL4A3(1285), COL4A4(1286), COL4A5(1287), COL4A6(1288)
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Analysis Note
An SDS polyacrylamide gel electrophoresis test run under reducing conditions consistent with basement membrane collagen yields three major bands.
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.
Disclaimer
This product should be stored desiccated at -20°C, and will retain activity in these conditions for 3 years.
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.
Preparation Note
This powder can be reconstituted in sterile .5 M acetic acid, PBS or water at 1 mg/mL. A PBS solution will be stable for at least one year at -20°C.
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Klasa składowania
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Jian Liu et al.
Stem cell research & therapy, 11(1), 348-348 (2020-08-14)
The biological role of miR-203 and the underlying mechanisms on the proliferation of epidermal stem cells (ESCs) have not yet been reported during the progression of chronic wound healing in diabetes mellitus. Our previous studies have observed that the expression
R Kalluri et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(13), 6201-6205 (1994-06-21)
Human Goodpasture syndrome is a lethal form of autoimmune disease that is characterized by pulmonary hemorrhage and glomerulonephritis. The tissue injury is mediated by autoantibodies that bind to glomerular and alveolar basement membrane. The target autoantigen is alpha 3(IV) collagen
Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis.
B G Hudson et al.
The Journal of biological chemistry, 268(35), 26033-26036 (1993-12-15)
Jiachao Yu et al.
Scientific reports, 10(1), 3695-3695 (2020-03-01)
In situ molecular imaging of protein films adsorbed on a solid surface in water was realized by using a vacuum compatible microfluidic interface and time-of-flight secondary ion mass spectrometry (ToF-SIMS). Amino acid fragments from such hydrated protein films are observed
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.
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