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Human Polyclonal MBOAT4 Primary Antibody for IF (p), IHC (p) - ABIN1714457
Yu, Chu, Chen, Hsieh, Kuo: Mediation of oxidative stress in hypothalamic ghrelin-associated appetite control in rats treated with phenylpropanolamine. in Genes, brain, and behavior 2016
Show all 2 Pubmed References
Human Polyclonal MBOAT4 Primary Antibody for ELISA, WB - ABIN4274728
Takahashi, Ida, Sato, Nakashima, Nakamura, Tsuji, Kojima: Production of n-octanoyl-modified ghrelin in cultured cells requires prohormone processing protease and ghrelin O-acyltransferase, as well as n-octanoic acid. in Journal of biochemistry 2009
MBOAT4 expression is significantly increased in Japanese patients with schizophrenia compared to controls.
Plasma GOAT levels exhibit high specificity/sensitivity to predict prostate carcinoma-presence compared with other PCa-biomarkers, especially in non-diabetic individuals.
The role of ghrelin O-acyltransferase cysteine residue in the ghrelin acylation
GOAT prefers n-hexanoyl-CoA over n-octanoyl-CoA as the acyl donor, although in the stomach the n-octanoyl form is the predominant form of acyl-modified ghrelin.
The GOAT active site was characterized by defining substrate-enzyme interactions used to bind and recognize ghrelin.
GOAT is also present in human plasma and GOAT protein levels depend on the metabolic environment with decreased levels in anorexic and increased levels in morbidly obese patients
Studies suggest that dysregulation in the components of the ghrelin system including ghrelin, ghrelin receptor (GHSR1a) and ghrelin-O-acyl-transferase can lead to or influence the development and/or progression of highly concerning pathologies.
Architectural organization of the metabolic regulatory enzyme ghrelin O-acyltransferase.
Data indicate that ghrelin O-acyltransferase (GOAT) mRNA and protein are expressed in the normal prostate and prostate cancer tissue samples.
Visceral adipose tissue from obese patients with type 2 diabetes showed higher levels of GOAT.
Genetic variation of the ghrelin activator gene ghrelin O-acyltransferase (GOAT) is associated with anorexia nervosa. (Review)
Identification of GOAT expression in various tissues support the concept that in addition to the important endocrine effect of acylated ghrelin, the paracrine effects of locally synthetised and acylated ghrelin may be important.
Based on the results of tjhis study concluded that genetic variation in GOAT might be implicated in the etiology of anorexia nervosa.
Modulation of GOAT or ghrelin signaling may be a clinically relevant strategy to treat metabolic diseases such as type II diabetes.
The presence of PC and GOAT in the cells, as well as n-octanoic acid in the culture medium, was necessary to produce n-octanoyl ghrelin.
The identification and characterization of human GOAT, the ghrelin O-acyl transferase, is reported.
GOAT was expressed in human immortalized chondrocyte cell lines and in human cultured primary chondrocytes.
Thus, the adipogenic action of exogenous unacylated ghrelin in tibial marrow is dependent upon acylation by GOAT and activation of GHS-R1a.
the effect of GOAT on gastric acid secretion and expression of ghrelin in vitro, were investigated.
Gene browse revealed QTL for body weight/size, genes involved in immune system, and two main protein-coding genes involved in the Glucose homeostasis, Mboat4 and Leprotl1. Heritability and coefficient of genetic variance (CVg) were 0.49 and 0.31 for females, while for males, these values 0.34 and 0.22, respectively.
GOAT immunoreactivity is aggregated at the base of the dentate granule cell layer in wild-type mice. This was not affected by the pharmacological inhibition of GHSR1a or the metabolic state-dependent fluctuation of systemic ghrelin levels. But it was absent in the GHSR1a knockout mouse hippocampus, implying that the expression of GHSR1a may be a prerequisite for the production of GOAT.
Both ghrelin and GOAT are localized primarily in the red pulp of the spleen. Importantly, in the thymus, ghrelin was predominantly localized to the medulla, whereas GOAT was found in the cortex, implying differing roles in T cell development. Both regulates obesity-induced inflammation.
anxiogenic actions of GOAT deletion not related to high plasma des-acyl ghrelin
GOAT knock-out pregnant mice on calorie-restricted diet are more prone to hypoglycemia than wild type.
circadian rhythmicity of ghrelin signaling requires Bmal1 and is driven by a food-responsive clock in the gastric ghrelin-secreting cell that not only regulates ghrelin, but also GOAT activity.
observations demonstrate that germline loss of ghrelin-O-acyltransferase alters Growth Hormone release and patterning
Altered lipid and salt taste responsivity in ghrelin and GOAT null mice.
The absence of GOAT does not alter glucose intolerance suggesting that desacyl/acyl ghrelin is not a major denominator for glucose homeostasis.
The absence of the enzyme GOAT does not play a significant role in maintenance of body core temperature or metabolic adaptation during exposure to low external temperatures.
GOAT induced ghrelin acylation regulates hedonic feeding.
The endogenous GOAT-ghrelin-growth hormone secretagogue receptor system is not essential for the maintenance of euglycemia during prolonged calorie restriction.
While there is considerable overlap in expression pattern between ghrelin and ghrelin O-acyltransferase (GOAT), the latter exhibits some unique tissue expression that could suggest that additional peptides may be acylated and await discovery.(Review)
This is the first report that the GOAT/ghrelin system regulates bile acid metabolism, and these findings suggest a novel function of GOAT in the regulation of intestinal bile acid reabsorption..
Ghrelin O-acyltransferase (GOAT) is essential for growth hormone-mediated survival of calorie-restricted mice
The present study demonstrates that stomach GOAT mRNA levels correlate with circulating acylated-ghrelin levels in fasted and diet-induced obese mice.
These data suggest species differences between rats and mice in gastric GOAT expression perhaps resulting in a different role of the MBOAT4 enzyme in the rat stomach.
Mediates the octanoylation of ghrelin at 'Ser-3'. Can use a variety of fatty acids as substrates including octanoic acid, decanoic acid and tetradecanoic acid.
O-acyltransferase (membrane bound) domain containing 4
, O-acyltransferase domain-containing protein 4
, ghrelin O-acyltransferase
, membrane-bound O-acyltransferase domain-containing protein 4