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Anticorps > 20231 - Purified freeze-dried antibody to chicken type II collagen

20231 - Purified freeze-dried antibody to chicken type II collagen



Chicken cartilage paraffin section, IHC


species

Chicken



immunogen

Type II collagen




Type II collagen is a fibrillar collagen composed of three identical α1(II) chains.  The type II collagen is found in cartilage and the vitreous humor of the eye. Mutations in this gene are associated with achondrogenesis, chondrodysplasia, early onset familial osteoarthritis, SED congenita, Langer-Saldino achondrogenesis, Kniest dysplasia, Stickler syndrome type I, and spondyloepimetaphyseal dysplasia Strudwick type. [according to RefSeq]

Immunogen : Native type II collagen extracted from chicken cartilage.

Host : Rabbit.

 

Polyclonal antibody purified by chromatography.

 

For research only.

Purified, freeze-dried antibody in 0.1 mL vials. Reconstitute with 0.1 mL distilled water and store aliquots at -20°C.

Unreconstituted

24 months at -20°C.

 

Reconstituted

Before use aliquot and store at -20°C (6 months). Avoid repeated freeze/thaw cycles.

Applications

IF, IHC, ELISA

 

Working dilutions

ELISA ≥ 1/2000 (OD = 0.5)

IF ≥ 1/40

IHC ≥ 1/500

Optimal dilutions should be determined by the end user.


Share your experience with this antibody in your specific application

  • #318j

Presentation

Type II collagen is a fibrillar collagen composed of three identical α1(II) chains.  The type II collagen is found in cartilage and the vitreous humor of the eye. Mutations in this gene are associated with achondrogenesis, chondrodysplasia, early onset familial osteoarthritis, SED congenita, Langer-Saldino achondrogenesis, Kniest dysplasia, Stickler syndrome type I, and spondyloepimetaphyseal dysplasia Strudwick type. [according to RefSeq]



Description

Immunogen : Native type II collagen extracted from chicken cartilage.

Host : Rabbit.

 

Polyclonal antibody purified by chromatography.

 

For research only.



Format

Purified, freeze-dried antibody in 0.1 mL vials. Reconstitute with 0.1 mL distilled water and store aliquots at -20°C.


Stability

Unreconstituted

24 months at -20°C.

 

Reconstituted

Before use aliquot and store at -20°C (6 months). Avoid repeated freeze/thaw cycles.


Use

Applications

IF, IHC, ELISA

 

Working dilutions

ELISA ≥ 1/2000 (OD = 0.5)

IF ≥ 1/40

IHC ≥ 1/500

Optimal dilutions should be determined by the end user.


Lots

  • #318j
    • IgG :

      4,4



      pH :

      7,8

      ELISA


      ELISA not tested with our current protocol.


      IF


      With fluorescein anti-rabbit IgG conjugate, optimal working dilution at 1/40 on frozen chicken cartilage tissues.


      IHC


      Immunoperoxidase technique with the Envision / Dako kit, 0.5% hyaluronidase pretreatment, optimal working dilution at 1/500 on fixed paraffin-embedded chicken cartilage.




References

  • «Immunohistochemical study of collagens of the extracellular matrix in cartilage of Sepia officinalis. Eur. J. Histochem. 1999, 43, 211-225.»
    Bairati A., Comazzi M., Gioria M., Hartmann D.J., Leone F., Rigo C.
  • «Processing of Type XI Collagen. J. Biol. Chem., 1996, 271, 23743-23748.»
    Rousseau J.C., Farjanel J., Boutillon M.M., Hartmann D.J., van der Rest M., Moradi-Ameli M.
  • «Bone organotypic culture method: a model for cytocompatibility testing of biomaterials. Cells and Materials 1994, 4, 113-123.»
    Anselme K., Lanel B., Gentil C., Hardouin P., Marie P.J., Sigot-Luizard M.F.
  • «Proteglycan and collagen synthesis are correlated with actin organization in dedifferentiating chondrocytes. Eur. J. Cell. Biol. 1991, 56, 364-373.»
    Mallein-Gerin F., Garrone R., Van der Rest M.
  • «Proteoglycan core protein and type II collagen gene expressions are not correlated with cell shape changes during low density chondrocyte cultures. Differentiation 1990, 43, 204-211.»
    Mallein-Gerin F., Ruggiero F., Garrone R.
  • «In vitro morphogenesis of chick embryo hypertrophic cartilage. J. Cell. Biol., 1987, 105, 999-1006.»
    Tacchetti C., Quarto R., Nitsch L., Hartmann D.J., Cancedda R.