Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells and is caused by caspase activation. Proteins that comprise the Bcl-2 family appear to control the activation of these enzymes. One such member is multi-domain antiapoptotic protein Bfl-1, which is overexpressed in stomach and other cancers. Bfl-1 can interact with Bax and suppress apoptosis by inhibiting the release of cytochrome c and caspase-3 activation. It is upregulated in cisplatin-resistant human bladder tumors, suggesting that its expression may be important for cisplatin resistance and inhibition of apoptosis in cancer cells. At least two isoforms of Bfl-1 are known to exist.
Recommended Dilutions: ELISA: 1:10,000-1:20,000; Immunohistochemsitry: 10 µg/mL; Immunofluorescence Microscopy: 20 µg/mL; Western Blot: 1 - 2 µg/mL; contains 0.02% (w/v) Sodium Azide
Type: Primary
Antigen: BCL2A1
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope: N-Terminal
Host: Rabbit
Isotype:
Reactivity: Human, Mouse, Rat