Technical Data
ADAM 15, CT (a Disintegrin and Metalloprotease 15, Metargidin, MDC15)
The ADAM (A Disintegrin and Metalloprotease) family of cell surface proteases mediate a number of cellular processes, including differentiation, cell fusion, cell-cell interactions, and shedding of plasma membrane-bound growth factor precursors1. Each ADAM contains a prodomain, a catalytic metalloprotease domain, a disintegrin domain, a transmembrane domain, and a cytoplasmic domain1. The cytoplasmic domain of ADAM15 is phosphorylated and interacts with Src family tyrosine kinases2. ADAM15 contains an RGD sequence within its disintegrin domain, and thus has been given the trivial name metargidin. In HUVEC, ADAM15 localizes to adherens junctions3. Although the mature ADAM15 has a molecular weight of 100 kD, ADAM family members can undergo proteolytic processing autocatalytically or by furin proteases to yield smaller molecular weight forms.

Suitable for use in Western Blotting. Other applications not tested.

Recommended Dilution:
Western blot: 1:500
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (30-50%). Freeze at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
100ug-20CBlue IceHumanRabbit
A synthetic peptide derived from the C-terminal end of the cytoplasmic domain of human ADAM15
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 50% glycerol, 0.09% sodium azide.
Recognizes the 100kD full-length form in HUVEC lysates, but other forms are possible in different cell and tissue types. Species Reactivity: Human
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Yamamoto, S. et al. (1999) Immunol. Today 20: 278-284. 2. Poghosyan, Z. (2002). J. Biol. Chem. 277: 4999-5007. 3. Ham, C. et al. (2002). Exp Cell Res. 279:239-47.