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Merck

C7974

Sigma-Aldrich

Monoclonal Anti-Collagen, Type X antibody produced in mouse

clone COL-10, ascites fluid

Synonym(e):

Anti-Col10, Anti-Col10a-1

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

ascites fluid

Antikörper-Produkttyp

primary antibodies

Klon

COL-10, monoclonal

Mol-Gew.

antigen 60 kDa (in denatured-reduced preparations)

Enthält

15 mM sodium azide

Speziesreaktivität

deer, human, pig

Methode(n)

dot blot: suitable
immunocytochemistry: 1:1,000 using HT 1080 human fibrosarcoma cells
western blot: suitable

Isotyp

IgM

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... COL10A1(1300)

Allgemeine Beschreibung

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.

Anwendung

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. Wirkung

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.

Haftungsausschluss

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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Empfehlung

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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)
Mohammad Mardani et al.
Iranian journal of basic medical sciences, 16(11), 1163-1169 (2014-02-05)
Platelet-rich plasma (PRP) has recently emerged as a promising strategy in regenerative medicine due to its multiple endogenous growth factors. Little is known about the role of PRP as a promoter in chondrogenesis of human adipose derived stem cells (hADSCs).
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)
Comprehensive Natural Products II: Chemistry and Biology, 489-489 (2010)

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