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demonstration that PPIP5K2 has a role in hearing in humans indicates that PP-IP signaling is important to hair cell maintenance and function within inner ear
This study characterized kinetic properties of the bifunctional inositol pyrophosphate 5-diphosphoinositol 1,2,3,4,6-pentakisphosphatekinase/inositol pyrophosphate, 1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate phosphatase activities of full-length diphosphoinositol pentakisphosphate kinase 1 and 2.
SEZ6L, HISPPD1, FEZF1, SAMD11 gene variants may be associated with autism spectrum disorder.
The degree of nuclear localization of hPPIP5K2 was increased when S1006 was rendered non-phosphorylatable by its mutation to Ala.
the specificity constants for PPIP5K2 revise upwards by one-to-two orders of magnitude the inherent catalytic activities of this enzyme, and we show its equilibrium point favours 80-90% depletion of InsP/-InsP.
describe the PPIP5K2's conformational dynamics, its unprecedented topological presentation of nucleotide and inositol phosphate, and the charge balance that facilitates partly associative in-line phosphoryl transfer
Inositol phosphates (IPs) and diphosphoinositol phosphates (PP-IPs), also known as inositol pyrophosphates, act as cell signaling molecules. HISPPD1 has both IP6 kinase (EC 126.96.36.199) and PP-IP5 (also called IP7) kinase (EC 188.8.131.52) activities that produce the high-energy pyrophosphates PP-IP5 and PP2-IP4 (also called IP8), respectively (Fridy et al., 2007
VIP1 homolog 2
, histidine acid phosphatase domain-containing protein 1
, inositol heptaphosphate kinase 2
, inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
, insP6 and PP-IP5 kinase 2
, histidine acid phosphatase domain containing 1