C7974
Monoclonal Anti-Collagen, Type X antibody produced in mouse
clone COL-10, ascites fluid
Synonyme(s) :
Anti-Col10, Anti-Col10a-1
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About This Item
Produits recommandés
Source biologique
mouse
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
ascites fluid
Type de produit anticorps
primary antibodies
Clone
COL-10, monoclonal
Poids mol.
antigen 60 kDa (in denatured-reduced preparations)
Contient
15 mM sodium azide
Espèces réactives
deer, human, pig
Technique(s)
dot blot: suitable
immunocytochemistry: 1:1,000 using HT 1080 human fibrosarcoma cells
western blot: suitable
Isotype
IgM
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... COL10A1(1300)
Description générale
Collagens are extracellular glycoproteins made up of three polypeptides that intermingle to form a triple helix. Type X collagen is a homotrimer of 59 kD α1(X) chains found in fetal hypertrophic cartilage in the growth zones of long bones, vertebrae and ribs, whereas in adults it is also present in thyroid cartilage. Monoclonal anti-collagen, type X antibody can be used in histological and immunohistochemical evaluation of cell cultures. It is also useful in study of specific differential tissue expression.
Monoclonal Anti-Collagen, Type X (mouse IgM isotype) is derived from the COL-10 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a BALB/c mouse immunized with porcine collagen type X. Collagen type X shares a similar domain structure with type VIII collagen: a central triple-helical (COL1) domain of 50 kDa is flanked by N-terminal (NC2) and C-terminal (NC1) non-triple-helical domains.
Immunogène
purified pig collagen type X.
Application
Monoclonal Anti-Collagen, Type X antibody produced in mouse has been used in
- enzyme linked immunosorbent assay (ELISA)
- dot-blot
- immunoblotting and
- immunohistochemistry
Actions biochimiques/physiologiques
Type X collagen is a product of hypertrophic chondrocytes. Type X collagen is non-fibrillar, but forms fine pericellular filaments in association with cartilage collagen. It interacts with matrix proteins, such as connexin V, chondrocalcein, collagen II and proteoglycans, as well as with Ca2+. It acts as a scaffold to avoid local collapse during endochondral ossification and also has a role in cartilage mineralization. Mutations in the NC1-encoding domain of the human α1(X) collagen gene, are associated with Schmid metaphysical chondroplasia.
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Réf. du produit
Description
Tarif
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Aasma A Khan et al.
Biotechnology progress, 25(2), 508-515 (2009-03-19)
The use of bioreactors for cartilage tissue engineering has become increasingly important as traditional batch-fed culture is not optimal for in vitro tissue growth. Most tissue engineering bioreactors rely on convection as the primary means to provide mass transfer; however
Christopher R Rowland et al.
Biomaterials, 91, 57-72 (2016-03-22)
The native extracellular matrix of cartilage contains entrapped growth factors as well as tissue-specific epitopes for cell-matrix interactions, which make it a potentially attractive biomaterial for cartilage tissue engineering. A limitation to this approach is that the native cartilage extracellular
Schmid type of metaphyseal chondrodysplasia and COL10A1 mutations?findings in 10 patients
Makitie O, et al.
American Journal of Medical Genetics. Part A, 137(3), 241-248 (2005)
Temporal and spatial modulation of chondrogenic foci in subchondral microdrill holes by chitosan-glycerol phosphate/blood implants
Chevrier A, et al.
Osteoarthritis and Cartilage, 19(1), 136-144 (2011)
Direct bone morphogenetic protein 2 and Indian hedgehog gene transfer for articular cartilage repair using bone marrow coagulates
Sieker JT, et al.
Osteoarthritis and Cartilage, 23(3), 433-442 (2015)
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