epitope corresponding to amino acids 61-212 of Bok (Bcl-2-related ovarian killer) of human origin
Modification Notes
Members of the Bcl-2 family of proteins interact to regulate apoptosis, a process by which multicellular organisms eliminate superflous cells. Various homodimers and heterodimers formed by proteins in this family either promote or inhibit apoptosis. Bcl-2 blocks cell death following a variety of stimuli and confers a death-sparing effect on certain hematopoietic cell lines following growth factor withdrawal. Bok, or Bcl-2 related ovarian killer, is highly expressed in ovary, testis, uterus and mammary glands. Bok induces apoptosis in cells, which is suppressible by anti-apoptotic human Bcl-2 family proteins. Bok targets mitochondria and triggers cytochrome c release through a caspase- independent mechanism. Bok contains the conserved Bcl-2 homology (BH) domains 1, 2 and 3, but lacks the BH4 domain. Bok selectively heterodimerizes with some anti-apoptotic members of the Bcl-2 protein family, including Mcl-1 and Bfl-1, but it does not appear to interact with Bcl-2, Bcl-x L and Bcl-w.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Bok of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including bovine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 61-212 of Bok (Bcl-2-related ovarian killer) of human origin
Tissue Specificity
epitope corresponding to amino acids 61-212 of Bok (Bcl-2-related ovarian killer) of human origin