Product nameAnti-ADAMTS15 antibody
See all ADAMTS15 primary antibodies
DescriptionRabbit polyclonal to ADAMTS15
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Human
Synthetic peptide based on the propeptide region of human ADAMTS-15 ADAMTS15.(Peptide available as ab45243.)
We have a range of domain specific antibodies for this target. For a full list please see all ADAMTS15 antibodies.
Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferpH: 7.40
Preservative: 0.05% Sodium azide
Constituents: PBS, 50% Glycerol, 2.9% Sodium chloride
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab45047 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Tissue specificityExpressed in fetal liver and kidney, but not in any of the adult tissues examined.
Sequence similaritiesContains 1 disintegrin domain.
Contains 1 peptidase M12B domain.
Contains 3 TSP type-1 domains.
DomainThe 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.
modificationsThe precursor is cleaved by a furin endopeptidase.
Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion.
Cellular localizationSecreted > extracellular space > extracellular matrix.
- Information by UniProt
- A disintegrin and metalloproteinase with thrombospondin motifs 15 antibody
- A disintegrin like and metalloprotease reprolysin type with thrombospondin type 1 motif 15 antibody
- A disintegrin like and metalloprotease reprolysin type with thrombospondin type 1 motif 15 preproprotein antibody
This product has been referenced in:
- McRae N et al. Glucocorticoids Improve Myogenic Differentiation In Vitro by Suppressing the Synthesis of Versican, a Transitional Matrix Protein Overexpressed in Dystrophic Skeletal Muscles. Int J Mol Sci 18:N/A (2017). Read more (PubMed: 29211034) »
- Dancevic CM et al. Biosynthesis and expression of a disintegrin-like and metalloproteinase domain with thrombospondin-1 repeats-15: a novel versican-cleaving proteoglycanase. J Biol Chem 288:37267-76 (2013). WB ; Human . Read more (PubMed: 24220035) »