Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H, M||IP, WB||Rb||Purified||Polyclonal Antibody|
|Presentation||0.07M Tris-glycine, pH 7.4, 0.105M NaCl, 0.035% sodium azide with 30% glycerol|
|Application||Anti-StIP-1 Antibody is a high quality Rabbit Polyclonal Antibody for the detection of StIP-1 & has been validated in IP & WB.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||2 years at -20°C|
|Material Size||200 µg|
|Anti-StIP-1 (rabbit polyclonal IgG) - 2116120||2116120|
|Anti-StIP-1 - 17528||17528|
|Reference overview||Pub Med ID|
|Purification and characterization of the human elongator complex.|
Hawkes, Nicola A, et al.
J. Biol. Chem., 277: 3047-52 (2002) 2002
Human Elongator complex was purified to virtual homogeneity from HeLa cell extracts. The purified factor can exist in two forms: a six-subunit complex, holo-Elongator, which has histone acetyltransferase activity directed against histone H3 and H4, and a three-subunit core form, which does not have histone acetyltransferase activity despite containing the catalytic Elp3 subunit. Elongator is a component of early elongation complexes formed in HeLa nuclear extracts and can interact directly with RNA polymerase II in solution. Several human homologues of the yeast Elongator subunits were identified as subunits of the human Elongator complex, including StIP1 (STAT-interacting protein 1) and IKAP (IKK complex-associated protein). Mutations in IKAP can result in the severe human disorder familial dysautonomia, raising the possibility that this disease might be due to compromised Elongator function and therefore could be a transcription disorder.
|A Stat3-interacting protein (StIP1) regulates cytokine signal transduction.|
Collum, R G, et al.
Proc. Natl. Acad. Sci. U.S.A., 97: 10120-5 (2000) 2000
Genetic and biochemical studies have led to the identification of the Stat3-Interacting Protein StIP1. The preferential association of StIP1 with inactive (i.e., unphosphorylated) Stat3 suggests that it may contribute to the regulation of Stat3 activation. Consistent with this possibility, StIP1 also exhibits an affinity for members of the Janus kinase family. Overexpression of the Stat3-binding domain of StIP1 blocks Stat3 activation, nuclear translocation, and Stat3-dependent induction of a reporter gene. These studies indicate that StIP1 regulates the ligand-dependent activation of Stat3, potentially by serving as a scaffold protein that promotes the interaction between Janus kinases and their Stat3 substrate. The ability of StIP1 to associate with several additional members of the signal transducer and activator of transcription family suggests that StIP1 may serve a broader role in cytokine-signaling events.