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C7974

Sigma-Aldrich

Monoclonal Anti-Collagen, Type X antibody produced in mouse

clone COL-10, ascites fluid

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Synonym(s):
Anti-Col10, Anti-Col10a-1
MDL number:
MFCD02686071
NACRES:
NA.41

biological source

mouse

Quality Level

200

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.

Q03692

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... COL10A1(1300)

Related Categories

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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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)
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
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)
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)
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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