Biotin Anti-Collagen IV antibody
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Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Biotin Anti-Collagen IV antibody (AB6581)
Immunohistochemical analysis of formalin-fixed paraffin-embedded human tissue sections, labelling Collagen IV with ab6581 at a concentration of 10 μg/mL for 1 hour at room temperature. The left panel is human kidney sections with the right panel being human liver sections. Antigen retrival was performed with 0.01 M sodium citrate buffer at pH 6.0 at 99°C for 20 mins. The secondary used was a rabbit peroxidase secondary antibody at a 1/10,000 dilution incubated for 45 mins at room temperature. Counterstaining against nuclear DNA was hematoxylin.
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At least 11 genetically distinct gene products are collectively referred to as 'collagen types' or other proteins and proteoglycans of the extracellular matrix. In humans, collagens are composed of about 20 unique protein chains which under go various types of post-translational modifications and are ultimately assembled into a triple helix. This results in great diversity between collagen types. Collagens are highly conserved throughout evolution and are characterized by an uninterrupted "Glycine-X-Y" triplet repeat that is a necessary part of the triple helical structure. For these reasons it is often extremely difficult to generate antibodies with specificities to collagens. The development of type specific antibodies is dependent on NON-DENATURED three-dimensional epitopes. This preparation results in a native conformation of the protein.
These antibodies are well suited to detect extracellular matrix proteins in normal as well as disease state tissues. Disruption of tissue organization is the hallmark of neoplasia. Malignant lesions can be distinguished from benign by examining the breakdown of basement membranes and loss of 3-dimensional architecture. Malignant cells are presumed to use matrix metalloproteases to degrade barriers created by the extracellular matrix which then allows metastasis to occur. Collagenases, stomelysins and gelatinases can collectively degrade all of the various components of the extracellular matrix, including fibrillar and non-fibrillar collagens and basement membrane glycoproteins.
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This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The highly organized network of collagen type IV plays a supreme role in maintaining the integrity and functionality of the basement membrane. It exists predominantly as part of a supramolecular complex associating with laminin nidogen and perlecan forming a multifunctional platform. This platform facilitates cellular signaling tissue elasticity and filtration functions. The basement membrane's selective permeability heavily relies on this network structure to regulate the exchange of molecules between tissues like blood vessels and epithelial sheets.
Pathways
Collagen IV contributes to several critical functions within the extracellular matrix organization and cell-matrix adhesion pathways. Specifically it interacts intimately with integrins and matrix metalloproteinases (MMPs) playing roles in angiogenesis and tissue repair. Additionally its interactions with other collagens and integrins within these pathways enhance cellular responses to mechanical stress and contribute to structural resilience in tissues.
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제품이 사용된 논문 (10)
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Journal of neuroinflammation 21:72 PubMed38521959
2024
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Journal of neuroinflammation 20:179 PubMed37516868
2023
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Fluids and barriers of the CNS 20:24 PubMed37013659
2023
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Stem cell research & therapy 9:324 PubMed30463594
2018
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Stem cell research & therapy 9:252 PubMed30257706
2018
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ACS applied materials & interfaces 8:21848-60 PubMed27136321
2016
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Molecular medicine reports 11:3734-40 PubMed25592406
2015
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Macromolecular bioscience 13:1135-49 PubMed23832790
2013
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IHC
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Journal of immunology (Baltimore, Md. : 1950) 189:2181-90 PubMed22844119
2012
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The Journal of neuroscience : the official journal of the Society for Neuroscience 32:9805-16 PubMed22815495
2012
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Mouse
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