The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Blocking - Blocking peptide for Anti-ADAMTS5 antibody (ab41037)
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions. - If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer. - Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent. - Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised. - Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.
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Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Information available upon request.
A disintegrin and metalloproteinase with thrombospondin motifs 11
A disintegrin and metalloproteinase with thrombospondin motifs 5
A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 5
A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase 2)
A disintegrin-like and metalloprotease with thrombospondin type 1 motif, 5
A Disintigrin And Metalloproteinase with ThromboSpondin motif-5
ADAM metallopeptidase with thrombospondin type 1 motif 5
ADAM TS 11
ADAM TS 5
Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.
Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.
The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
The precursor is cleaved by a furin endopeptidase.
Secreted > extracellular space > extracellular matrix.