• Product nameAnti-ADAMTS9 antibody
    See all ADAMTS9 primary antibodies
  • Description
    Rabbit polyclonal to ADAMTS9
  • Tested applicationsNeutralising, WBmore details
  • Species reactivity
    Reacts with: Mouse, Human
    Predicted to work with: Rat
  • Immunogen

    Synthetic peptide based on the propeptide region of human ADAMTS9. (Peptide available as ab41244.)


Associated products


Our Abpromise guarantee covers the use of ab28279 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
Neutralising Use at an assay dependent dilution. PubMed: 20551050To neutralize the effects of extracellular ADAMTS9.
WB 1/1000 - 1/5000. Predicted molecular weight: 217, 183 , 121 kDa.Can be blocked with ADAMTS9 peptide (ab41244). EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen.


  • RelevanceADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. ADAMTS9 is closest in homology to ADAMTS20, sharing 54% overall identity, and like ADAMTS20 ADAMTS9 gas a GON like domain at the carboxyterminal end. The GON domain at the carboxyterminal end is similar to the GON1 protein in C. elegans, mutations of which lead to defective gonadal development. ADAMTS9 is expressed in ovary and testis, but little is known about the role of ADAMTS9 in reproductive organs. ADAMTS9 is also expressed in the heart, placenta, lung, skeletal tissue, and pancreas, so the protein must have wider functions than just gonadal development. ADAMTS9, like ADAMTS20, has a total of 15 thrombospondin like domains. The first TS domain begins shortly after the catalytic and disintegrin domains. TS domains 2 to 6 follow a spacer domain, followed by linker domain 1, then TS domains 7 & 8, linker domain 2, and then TS domains 9 to 15. In other ADAMTS proteins the TS motifs are thought to bind to the ECM. The ADAMTS proteins contain at least one prohormone convertase cleavage site, although it appears that one site is used preferentially, and cleavage of the propeptide domain at this site generates active enzymes. For ADAMTS9, this site is the RRTKR sequence, and the mature ADAMTS9 has an aminoterminal sequence of FLSYPR. The catalytic site of ADAMTS9 is most like ADAMTS1, 14 and 15, with an HExxHVFNMxH sequence, perhaps giving these enzymes some shared specificity.
  • Cellular localizationSecreted protein; extracellular space; extracellular matrix.
  • Database links
  • Alternative names
    • A disintegrin and metalloproteinase with thrombospondin motifs 9 antibody
    • A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 9 antibody
    • A disintegrin like and metalloprotease with thrombospondin type 1 motif 9 antibody
    • ADAM metallopeptidase with thrombospondin type 1 motif 9 antibody
    • ADAM TS 9 antibody
    • ADAM TS9 antibody
    • ADAMTS 9 antibody
    • FLJ42955 antibody
    • KIAA1312 antibody
    see all

References for Anti-ADAMTS9 antibody (ab28279)

This product has been referenced in:
  • Demircan K  et al. ADAMTS4 and ADAMTS5 Knockout Mice Are Protected from Versican but Not Aggrecan or Brevican Proteolysis during Spinal Cord Injury. Biomed Res Int 2014:693746 (2014). WB ; Mouse . Read more (PubMed: 25101296) »
  • Demircan K  et al. ADAMTS1, ADAMTS5, ADAMTS9 and aggrecanase-generated proteoglycan fragments are induced following spinal cord injury in mouse. Neurosci Lett 544:25-30 (2013). WB ; Mouse . Read more (PubMed: 23562508) »

See all 3 Publications for this product

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Thanks for your call yesterday and for your patience while I have been in touch with the lab about ab28279. Unfortunately there are not any Western blot images to send, but the antibody was used in one publication which I have attached to this email. T...

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