CD11a is the alphaL protein subunit of LFA-1, paired with the shared beta2 chain CD18. The assembled integrin participates in leukocyte adhesion, including binding to ICAM-1. It is distinct from CD11b, the alpha partner in Mac-1; detecting the common beta chain does not identify which receptor is present.
Adhesive behavior can change without simply inventing a new receptor. A 1989 experiment showed that cross-linking the T-cell receptor rapidly and transiently increased adhesion through LFA-1. The authors connected signaling at the antigen receptor with altered adhesive function at another membrane complex.[ref]
For an illustrative comparison, measure surface CD11a and cell attachment before stimulation, shortly afterward and after recovery. A time-dependent attachment change need not be proportional to a change in receptor count. Molecular abundance, assembly with CD18 and functional adhesive state are separate measurements; a useful experiment states which one it actually observed.

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