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COL13A1 encodes the alpha chain of one of the nonfibrillar collagens. Additionally we are shipping COL13A1 Antibodies (24) and COL13A1 Proteins (4) and many more products for this protein.
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The combination of constitutively low expression of COL13A1, high physiological and metabolic demands, and consequentially relatively high exposure to stressors may explain the particular vulnerability of inferior rectus to thyroid-associated ophthalmopathy.
We identified overexpression of collagen type XIII alpha 1 in active Thyroid-associated ophthalmopathy affected fat.
Congenital myasthenic syndrome type 19 is caused by mutations in COL13A1.
The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin (show FN1 ELISA Kits), nidogen-2 (show NID2 ELISA Kits), perlecan (show HSPG2 ELISA Kits), and heparin.
two widely separated coiled-coil domains of type XIII (show UGDH ELISA Kits) and related collagens function as independent oligomerization domains participating in the folding of distinct areas of the molecule.
Data show that the induction of collagen XIII (show UGDH ELISA Kits) in endothelial cells of Alport syndrome kidneys mediates the selective recruitment of alpha1beta1 integrin-positive monocytes.
Collagen XIII (show UGDH ELISA Kits) plays an autocrine role in postsynaptic maturation, organization, and function of the vertebrate neuromuscular junction.
Cardiac dysfunction is reported in transgenic mouse fetuses overexpressing shortened type XIII collagen.
This gene encodes the alpha chain of one of the nonfibrillar collagens. The function of this gene product is not known, however, it has been detected at low levels in all connective tissue-producing cells so it may serve a general function in connective tissues. Unlike most of the collagens, which are secreted into the extracellular matrix, collagen XIII contains a transmembrane domain and the protein has been localized to the plasma membrane. The transcripts for this gene undergo complex and extensive splicing involving at least eight exons. Like other collagens, collagen XIII is a trimer\; it is not known whether this trimer is composed of one or more than one alpha chain isomer. A number of alternatively spliced transcript variants have been described, but the full length nature of some of them has not been determined.
collagen alpha-1(XIII) chain
, procollagen, type XIII, alpha 1
, type XIII collagen