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anti-Human Aspartate beta Hydroxylase Antibodies:
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The mRNA expression and promoter methylation rate of ASPH gene may play a role in the development and progression of breast cancer.
the role of FTH1 in the FIH control of HIF-1 activity, is reported.
the hydroxylase activity of ASPH affected HCC metastasis through interacting with vimentin and regulating EMT. As such, ASPH might be a promising therapeutic target of HCC.
Higher levels of HAAH/humbug mRNA were found in the hepatocellular carcinoma tissues relative to the adjacent cancerfree tissue.
this study provides evidence that ASPH is mutated in a distinct form of syndromic ectopia lentis.
Data show that junctate (ASPH) is an interacting partner of Orai1-STIM1 complex.
Ca(2+) and JNT-dependent disassembly of the CSQ2 polymer
Aspartyl-asparaginyl-beta-hydroxylase is an important, positive regulator of trophoblastic cell motility, and it's inhibition in vivo leads to impaired implantation and fetal growth, and alters Notch-signaling mechanisms.
Low expression of AAH in the endochylema and nucleus of trephocyte may play a role in patients with missed abortion.
role of gene in neuroblastoma cell motility
AAH over-expression may contribute to the infiltrative growth pattern of cholangiocarcinoma cells by promoting motility.
junctate has a role in calcium homeostasis in eukaryotic cells
This review summarizes recent progress in elucidating the molecular mechanisms of hypoxia-inducible factor (HIF)-1 activation, focusing on the role of oxygen-dependent prolyl hydroxylase in hypoxia signal transduction.
Overexpression of aspartyl beta-hydroxylase plays a role in the development and progression of hepatocellular carcinoma.
enhanced AAH gene activity is a common feature of human hepatocellular carcinoma and growth factor signaling through IRS-1 regulates AAH expression and increases cell motility and invasion
Human aspartyl (asparaginyl) beta-hydroxylase (HAAH) mRNA is overexpressed in biliary cancer cell lines and possibly involved in the pathogenesis of bile duct cancer.
Abundant AAH expression in trophoblasts as well as in decidua and endometrial glands, with reduced expression in spontaneous abortion and small-for-gestational-age term deliveries, suggesting that AAH may serve as a biomarker of impaired implantation.
Study demonstrates that high levels of humbug immunoreactivity in colon carcinomas correlate with histologic grade and tumor behavior, suggesting that humbug can serve as a prognostic biomarker.
AAH and Humbug are over-expressed in SH-Sy5y neuroblastoma cells, and their mRNAs are regulated by insulin/IGF-1 signaling through Erk MAPK, PI3 kinase-Akt, and Cdk-5, which are known mediators of cell migration.
Expression analysis showed that the mRNA expression level of humbug was correlated with invasive potential in various human gastric cancer cell lines.
Results predict that junctin ablation, or mutations that alter its structural attributes, may mimic the etiology of catecholaminergic polymorphic ventricular tachycardia by causing enhanced diastolic Ca2+ leak in the presence of beta-adrenergic activation.
in skeletal muscle the disruption of Tdn/CASQ link has a more profound effect on jSR architecture and myoplasmic Ca(2+) regulation than Jct/CASQ association.
junctate may play an important role in the regulation of sarcoplasmic reticulum Ca(2+) cycling through the interaction with SERCA2a in the murine heart.
evaluation of role in vivo
Cardiac remodeling and atrial fibrillation in transgenic mice overexpressing junctin
the N-terminus of junctate interacts with the C-terminus of TRPC2
To gain more insight into the underlying mechanisms of impaired contractile relaxation in transgenic mice with cardiac-specific overexpression of junctin (TG), we studied cellular Ca(2+) handling in these mice.
Junctin is an essential regulator of sarcoplasmic reticulum Ca release and contractility in normal hearts. Ablation of junctin is associated with aberrant Ca homeostasis, which leads to fatal arrhythmias
Data suggest that junctate over-expression is associated with an increase in the sarcoplasmic reticulum Ca2+ storage capacity and releasable Ca2+ content and support a physiological role for junctate in intracellular Ca2+ homeostasis.
review of recent findings concerning the expressional regulations and the proposed functions of junctin and junctate
Junctate-1 in the heart is closely linked to the homeostasis of E-C coupling proteins and a sustained increase of junctate-1 expression leads to a severe cardiac remodeling and arrhythmias.
involved in maintaining sarcoplasmic reticulum Ca2+ store size in skeletal myotubes
Partial downregulation of junctin enhances cardiac calcium cycling without eliciting ventricular arrhythmias in mice.
analysis of aspartyl (asparaginyl) beta-hydroxylase monoclonal antibodies
This gene is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis.
A beta H-J-J
, ASP beta-hydroxylase
, aspartyl/asparaginyl beta-hydroxylase
, cardiac junctin
, peptide-aspartate beta-dioxygenase
, aspartate beta-hydroxylase
, aspartyl beta-hydroxylase
, calsequestrin-binding protein
, junctional sarcoplasmic reticulum protein