SUMMARY, EXPLANATION AND LIMITATIONS:
The anti-Bcl-2α recognizes an human oncoprotein of 25-26 kDa that inhibits programmed cell death (apoptosis). Shows no cross reaction with protein Bcl-x or Bax or reacts to Bcl-2 murine or rat. Apoptosis is the physiological process by which all living organisms selectively eliminate cells that no longer need it are damaged or show serious genetic abnormalities. Therefore, defects in the control of this complex process have been linked both to cancer or autoimmune diseases from abnormal cells protected from the same degenerative diseases as multiple premature death of cells that should be safeguarded against it. In most follicular lymphomas, neoplastic germinal centers express high levels of Bcl-2α protein, whereas the normal or hyperplastic germinal centers are negative.
Immunogen: A synthetic peptide, aminoacids 41-54 (GAAPAPGIFSSQPG-Cys) of human Bcl-2 protein.
Staining pattern: Cytoplasm and cell membrane.
Positive control: Tissue sample from tonsil or follicular lymphoma.
This antibody is designed for the specific localization of human Bcl-2α using IHC techniques in formalin-fixed, paraffin-embedded tissue sections.
In normal lymphoid tissue, the anti-Bcl-2 reacts with B lymphocytes small follicular mantle zone and numerous small lymphoid cells within the areas T. The cells are stained in the germinal center corresponding to T helper cells that physiologically colonize it. In the thymus cells are colored some of the core while in the cortex immunostaining is weak or nonexistent. In hematopoietic tissues often stained some cells represent primarily reactive infiltration of leukocytes. For use as an evolutionary marker of malignancy has been reported that the expression or absence is of independent prognostic value in non-Hodgkin lymphoma B large cell carcinomas of the breast and lung tumors among many others.