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The protein encoded by this protein regulates inositol phosphate metabolism by phosphorylation of second messenger inositol 1,4,5-trisphosphate to Ins(1,3,4,5)P4. Additionally we are shipping ITPKB Antibodies (46) and many more products for this protein.
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These data identify Itpkb as an essential mediator of T cell activation and suggest Itpkb inhibition as a novel approach to treat autoimmune disease.
Itpkb controls hematopoietic stem cell homeostasis and prevent death from severe anemia in mice.
Itpkb controls survival, proliferation and cytokine production in mouse peripheral T cells.
Data present the structure of the complete catalytic domain of inositol 1,4,5-trisphophate 3-kinase B, including the CaM (show Calm2 Proteins) binding domain in complex with Mg(2 (show MCOLN1 Proteins)+) and ATP.
These data show that the absence of expression of the three isoenzymes of Itpk does not prevent the formation of IP5 and IP6 (show GPRIN2 Proteins), at least in mouse embryonic fibroblasts.[Itpka (show ITPKA Proteins), Itpkb, Itpkc (show ITPKC Proteins)]
Itpkb and inositol tetrakisphosphate mediate a survival signal in B cells.
B cells from Itpkb(-/-) Ig hen (show RPS6 Proteins) egg lysozyme (show LYZ Proteins) mice possess an anergic phenotype, hypoproliferate in response to cognate Ag, and yet they exhibit enhanced Ag-induced calcium signaling
ITPKB is increased in Alzheimer's brain three-fold in the cerebral cortex of most patients with Alzheimer's disease compared with control subjects and accumulates in dystrophic neurites associated with amyloid plaques.
a specific increase in inositol 1,4,5-trisphosphate 3-kinase A (show ITPKA Proteins) and B (ITPKA (show ITPKA Proteins) and ITPKB) was observed upon hESCs spontaneous differentiation.
IP3KB not only regulates cytoplasmic Ca(2 (show CA2 Proteins)+) signals by phosphorylation of subplasmalemmal and cytoplasmic Ins (show INS Proteins)(1,4,5)P(3) but may also be involved in modulating nuclear Ca(2 (show CA2 Proteins)+) signals generated from these nuclear envelope invaginations.
results highlight the potential role of the three isoforms of InsP3 3-kinase as direct InsP3 metabolizing enzymes and direct regulators of Ca2 (show CA2 Proteins)+ responses to extracellular signals
We aim to summarize the existing information about functionally uncoupled IP(3)R (show ITPR1 Proteins) and RyR channels, and to discuss the concept that those channels can participate in Ca(2 (show CA2 Proteins)+)-leak pathways.
In each of the three isoforms a nuclear export signal has evolved in the catalytic domain either de novo (IP3K-A (show ITPKA Proteins)) or as a substitute for an earlier evolved corresponding N-terminal signal (IP3K-B and IP3K-C (show ITPKC Proteins)).
The protein encoded by this protein regulates inositol phosphate metabolism by phosphorylation of second messenger inositol 1,4,5-trisphosphate to Ins(1,3,4,5)P4. The activity of this encoded protein is responsible for regulating the levels of a large number of inositol polyphosphates that are important in cellular signaling. Both calcium/calmodulin and protein phosphorylation mechanisms control its activity.
inositol-trisphosphate 3-kinase B
, inositol 1,4,5-trisphosphate 3-kinase B
, 1D-myo-inositol-trisphosphate 3-kinase B
, inositol-trisphosphate 3-kinase B-like
, IP3 3-kinase B
, IP3K B
, insP 3-kinase B
, proliferation-inducing protein 37