C7974
Monoclonal Anti-Collagen, Type X antibody produced in mouse
clone COL-10, ascites fluid
Synonym(s):
Anti-Col10, Anti-Col10a-1
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About This Item
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
COL-10, monoclonal
mol wt
antigen 60 kDa (in denatured-reduced preparations)
contains
15 mM sodium azide
species reactivity
deer, human, pig
technique(s)
dot blot: suitable
immunocytochemistry: 1:1,000 using HT 1080 human fibrosarcoma cells
western blot: suitable
isotype
IgM
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... COL10A1(1300)
General description
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.
Immunogen
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
Biochem/physiol Actions
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.
Disclaimer
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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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (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
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)
Discoidin domain receptor-1 deficiency attenuates atherosclerotic calcification and smooth muscle cell-mediated mineralization
Ahmad PJ, et al.
The American Journal of Pathology, 175(6), 2686-2696 (2009)
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