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The protein encoded by AHCYL1 interacts with inositol 1,4,5-trisphosphate receptor, type 1 and may be involved in the conversion of S-adenosyl-L-homocysteine to L-homocysteine and adenosine. Additionally we are shipping AHCYL1 Antibodies (38) and AHCYL1 Kits (3) and many more products for this protein.
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These results suggest that by inhibiting Bcl2l10 (show BCL2L10 Proteins) activity and promoting contact between endoplasmic reticulum and mitochondria, IRBIT facilitates massive Ca(2 (show CA2 Proteins)+) transfer to mitochondria and promotes apoptosis.
IRBIT forms signaling complexes with PIPKIalpha and NBCe1 (show SLC4A4 Proteins)-B, whose activity is regulated by PI(4,5)P2.
Formation of the Ribonucleotide reductase-IRBIT complex is regulated through phosphorylation of IRBIT, and ablation of IRBIT expression in HeLa cells causes imbalanced dNTP pools and altered cell cycle progression.
IRBIT is a master regulator of ion channels and ion transporters. (Review)
IRBIT plays an important role in intracellular pH regulation, mediated by NHE3 (show SLC9A3 Proteins), and further regulated by SPAK (show STK39 Proteins).
relationships between the WNK/SPAK (show STK39 PLURAL_@35658@) and IRBIT/PP1 (show PPA1 PLURAL_@35658@) sites in the regulation of Na+-HCO3- cotransporters
conclude that AHCYL1 expression is associated with ovarian carcinogenesis as an oncogene (show RAB1A Proteins) in chickens, whereas it plays the role of tumor suppressor in human EOC, suggesting a paradoxical function of AHCYL1 in ovarian carcinogenesis
A NBCe1 (show SLC4A4 Proteins)-B construct that lacks amino acid residues 2-16 of the amino-terminus is fully autoinhibited, but cannot be stimulated by IRBIT, indicating that autoinhibitory and IRBIT-binding determinants within the cytosolic amino-terminus are not identical.
Both IRBIT (inositol 1,4,5-trisphosphate receptor-binding protein) and WNK [with no lysine (K)] kinase have been implicated as additional HCO(3)(-) secretory controllers.
IRBIT opposes the effects of WNKs and SPAK (show STK39 Proteins) by recruiting PP1 (show PPA1 Proteins) to the complex to dephosphorylate CFTR (show CFTR Proteins) and NBCe1 (show SLC4A4 Proteins)-B, restoring their cell surface expression, in addition to stimulating their activities
AHCYL1 has a different function from AHCY (show AHCY Proteins) and plays an important role in embryogenesis by modulating inositol 1,4,5-trisphosphate receptor function for the intracellular calcium release
NHERF1 (show SLC9A3R2 Proteins) mediates ANG II (show AGT Proteins)-induced activation of renal NHE3 (show SLC9A3 Proteins), which requires coordination between IRBIT and the NHERF1 (show SLC9A3R2 Proteins) PDZ1 domain in binding and transporting NHE3 (show SLC9A3 Proteins)
IRBIT suppresses CaMKIIalpha activity and contributes to catecholamine homeostasis through TH phosphorylation.
Irbit was sequestered by InsP3 receptors (IP3Rs) in the endoplasmic reticulum
IRBIT opposes the effects of WNKs and SPAK (show STK39 Proteins) by recruiting PP1 (show PPP1CC Proteins) to the complex to dephosphorylate CFTR (show CFTR Proteins) and NBCe1 (show SLC4A4 Proteins)-B, restoring their cell surface expression, in addition to stimulating their activities
IRBIT can directly interact with the IP3R (show ITPR1 Proteins), and that both the suppressor domain and the IP3-binding core of the IP3R (show ITPR1 Proteins) are essential for a strong interaction.
phosphorylation of Ser71 and Ser74 were sufficient to enable inhibition of IP3 binding to the IP3R (show ITPR1 Proteins) by IRBIT
Data show that pNBC1 activation requires the IRBIT PEST domain, while CFTR (show CFTR Proteins) activation requires multiple domains, and suggest that IRBIT is a key coordinator of epithelial fluid and HCO3- secretion.
Results sugest that IRBIT modulates the polyadenylation state of specific mRNAs, both by controlling the cytoplasmic/nuclear partitioning of Fip1 (show RRAGA Proteins) and by inhibiting PAP (show ASAP1 Proteins) activity, in response to a stimulus that alters its phosphorylation state.
The protein encoded by this gene interacts with inositol 1,4,5-trisphosphate receptor, type 1 and may be involved in the conversion of S-adenosyl-L-homocysteine to L-homocysteine and adenosine. Several transcript variants encoding two different isoforms have been found for this gene.
, putative adenosylhomocysteinase 2-like
, S-adenosylhomocysteine hydrolase-like 1
, putative adenosylhomocysteinase 2
, DC-expressed AHCY-like molecule
, S-adenosyl homocysteine hydrolase homolog
, S-adenosyl-L-homocysteine hydrolase 2
, S-adenosylhomocysteine hydrolase-like protein 1
, adoHcyase 2
, dendritic cell expressed AHCY-like protein
, inositol 1,4,5-trisphosphate receptor-binding protein
, IP3R binding protein released with inositol 1,4,5-trisphosphate
, IP3R-binding protein released with inositol 1,4,5-trisphosphate
, S-adenosylhomocysteine hydrolase, related sequence 3