Background: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK-1 and RIP, are mediators of apoptosis. A novel serine/threonine kinase that mediates apoptosis was recently identified and designated ZIP kinase1. ZIP kinase contains an N-terminal kinase domain and a C-terminal leucine zipper structure and binds to ATF4 that is a member of ATF/CREB family. ZIP kinase has high sequence homology to DAP kinase (death-associated protein kinase), which is a mediator of apoptosis induced by gamma interferon. Overexpression of ZIP kinase induces apoptosis. ZIP and DAP kinases represent a novel kinase family, which mediates apoptosis through their catalytic activities. The messenger RNA was ubiquitously expressed in various tissues1.
Positive Control: Jurkat and HeLa whole cell lysates.
Purification Method: Antigen Immunoaffiinity Purification.
Source: Antibody raised in rabbits against a synthetic protein corresponding to amino acids 279 to 298 of the human ZIP kinase protein.
References: 1. Kawai T, et al. 'ZIP kinase, a novel serine/threonine kinase which mediates apoptosis.' Mol. Cell. Biol. 1998, 18, 1642-1651.
UniProt: O43293.
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
English
Deutsch
