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(Received for publication, March 20, 1995; and in revised form, April 26, 1995) From the We screened monoclonal antibodies to cell-surface proteins and
selected an antibody, called 6H1, that recognizes a putative
integrin-associated protein. The 6H1 monoclonal antibody (mAb)
indirectly coprecipitated
Volume 270,
Number 30,
Issue of July 28, pp. 17784-17790, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and/or
, but not
, or 
from Brij 96 detergent lysates of multiple cell lines. Large
scale purification using the 6H1 mAb yielded a single protein of
45-60 kDa with an amino-terminal sequence that exactly matched
CD63. Confirming that the 6H1 mAb recognized the CD63 protein, 6H1 and
a known anti-CD63 mAb yielded identical coprecipitation results and
identical colocalization into lysosomal granules containing cathepsin
D. Furthermore, we used an established anti-CD63 mAb to detect this
protein in an immunoprecipitate, and
also we observed VLA-3 and CD63 colocalization in cellular
``footprints.'' Notably, the cytoplasmic domain of
was neither required nor sufficient for CD63
association, suggesting that it occurred elsewhere within the
complex. Knowledge of these specific
CD63- and
CD63- biochemical associations should
lead to critical insights into the specialized functions of
, ,
and CD63.
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