This antibody recognises Collagen Type V and it has negligible cross-reactivity with Type I,II, III, IV, or VI collagens. Non-specific cross reaction with other human serum proteins or non-collagen extracellular matrix proteins is negligible.
This antibody was prepared by immunoaffinity chromatography using immobilized antigens followed by extensive cross-adsorption against other collagens, human serum proteins and non-collagen extracellular matrix
proteins to remove any unwanted specificities.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ELISA: 1/4000 - 1/8000.
IHC-Fr: 1/50 - 1/200.
IP: Use at an assay dependent dilution.
WB: 1/5000 - 1/10,000. Predicted molecular weight: 180 kDa.
Denaturing and reducing conditions will greatly diminish reactivity and selectivity of this antibody.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
Ehlers-Danlos syndrome 1 Ehlers-Danlos syndrome 2
Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 laminin G-like domain.
The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Sulfated on 40% of tyrosines.
Secreted > extracellular space > extracellular matrix.
Tamaki T et al. Qualitative alteration of peripheral motor system begins prior to appearance of typical sarcopenia syndrome in middle-aged rats. Front Aging Neurosci6:296 (2014).
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