Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
PAM encodes a multifunctional protein. Zusätzlich bieten wir Ihnen PAM Antikörper (28) und PAM Proteine (10) und viele weitere Produktgruppen zu diesem Protein an.
Showing 4 out of 10 products:
The ancient ability of PAM to localize to ciliary membranes, which release bioactive ectosomes, may be related to its ability to accumulate in intralumenal vesicles and exosomes
PAM expression is increased in the secretory pathway of differentiated neurons.
Oxygen Sensitivity of the Peptidylglycine alpha-Amidating Monooxygenase (PAM) in Neuroendocrine Cells
Two missense variants in PAM, encoding p.Asp563Gly (frequency of 4.98%) and p.Ser539Trp (frequency of 0.65%), confer moderately higher risk of type 2 diabetes (OR = 1.23, P = 3.9 x 10(-10) and OR = 1.47, P = 1.7 x 10(-5), respectively)
Detail the production of the catalytic core of human peptidylglycine alpha-hydroxylating monooxygenase (hPHMcc) in Escherichia coli possessing a N-terminal fusion to thioredoxin (Trx (zeige TXN ELISA Kits)).
Data indicate that catalytic inactivation of PHM caused by pH changes is accompanied by structural change between two states of the protein involving strong Cu-S interaction that does not involve M314.
nuclear retention of PAM mRNA is lost upon expressing the La proteins that lack a conserved nuclear retention element, suggesting a direct association between PAM mRNA and La protein in vivo
Disruption of AP-1 (zeige JUN ELISA Kits)-dependent late endosomal trafficking diminishes the ability of PAM to retain copper and produce amidated peptides.
deficits in PAM reversibly affect copper homeostasis, with behavioral and physiological consequences
Reduced amygdalar expression of Atox-1 and Atp7a (zeige ATP7A ELISA Kits) in PAM heterozygous mice may lead to reduced synaptic Cu levels, contributing to the behavioral and neurochemical alterations seen in these mice.
While glycine-extended reaction intermediates accumulated in the PAM(+/-) mice and reflected dietary copper availability, amidated products were far more prevalent under the conditions examined.
Although the copper-dependent mechanisms through which the endocytic trafficking of PAM alters gene expression have not been elucidated in this review, the cytosolic fragment of PAM identified in pituitary and atrial nuclei is likely to play a key role.
Cleavage of PAM releases a soluble CD fragment that localizes to the nucleus. Localization of PAM-CD to the nucleus was decreased when PAM-CD with phosphomimetic mutations was examined and when active Uhmk1 was simultaneously overexpressed.
Altered copper homeostasis in PAM(+/-) mice suggested a role for PAM in the cell type specific regulation of copper metabolism.
In 12-day-old (P12 (zeige CDK2AP1 ELISA Kits)) mouse pups derived from dams that began Cu deficiency on day 7 of gestation, there was a parallel reduction in brain PAM activity and protein of 40-50%.
expression analysis of PHM in rats and in mouse cells
This gene encodes a multifunctional protein. It has two enzymatically active domains with catalytic activities - peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). These catalytic domains work sequentially to catalyze neuroendocrine peptides to active alpha-amidated products. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene but some of their full length sequences are not yet known.
, peptidyl gycine alpha hydroxylating monooxygenase
, peptidylglycine alpha-hydroxylating monooxygenase
, peptidylglycine-alpha-hydroxylating monooxygenase
, peptidylglycine alpha-amidating monooxygenase
, peptidyl-glycine alpha-amidating monooxygenase
, peptidyl-glycine alpha-amidating monooxygenase-like
, pancreatic peptidylglycine alpha-amidating monooxygenase
, peptidyl alpha-amidating enzyme
, peptidyl-alpha-hydroxyglycine alpha-amidating lyase
, peptidylamidoglycolate lyase
, peptidylglycine 2-hydroxylase
, PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE PRECURSOR (PAM)