GOAT Immunoglobulin G1,IgG1 ELISA Kit
- Known as:
- GOAT Immunoglobulin G1,IgG1 Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- E0007GO
- Product Quantity:
- 48T
- Category:
- Elisa Kits
- Supplier:
- JING
- Gene target:
- GOAT Immunoglobulin G1 IgG1 ELISA Kit
Ask about this productRelated genes to: GOAT Immunoglobulin G1,IgG1 ELISA Kit
- Gene:
- MBOAT4 NIH gene
- Name:
- membrane bound O-acyltransferase domain containing 4
- Previous symbol:
- OACT4
- Synonyms:
- FKSG89, GOAT
- Chromosome:
- 8p12
- Locus Type:
- gene with protein product
- Date approved:
- 2005-09-27
- Date modifiied:
- 2015-08-25
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- Benign prostatic hyperplasia (BPH) affects aging men worldwide. Type 2 diabetes mellitus (T2DM) and BPH are aging related progressive diseases. High glucose (HG) promoted epithelial mesenchymal transformation (EMT) glucose-dependently in BPH cells. Arctigenin has multiple therapeutic functions as anti-tumor and anti-inflammatory. The role of Arctigenin in BPH and mechanism remain to be investigated. We proposed to explore the therapeutic effect of Arctigenin on BPH accompanied with T2DM and the molecular mechanism. EMT-related markers such as E-Cadherin and Vimentin along with Ki67 and MBOAT4/(acylated) Ghrelin/GHS-R in samples from BPH patients with euglycemia or T2DM were measured and the role of Arctigenin in cell proliferation, migration and vascular-like networks formation of BPH and vascular endothelial cells in HG culture and db/db mice (T2DM) with BPH were explored. Our results demonstrated that positive EMT-markers, MBOAT4/(acylated) Ghrelin/GHS-R and cell proliferation were found in HG samples of BPH patients, HG-induced cells and db/db mice. Arctigenin suppresses cell proliferation, cell migration and EMT, angiogenesis formation and attenuates BPH in mice under normal or HG condition. Our study suggested that Arctigenin might alleviate BPH companied with type 2 diabetes mellitus by inhibiting Ghrelin-induced EMT and cell proliferation through regulating MBOAT4/(acylated) Ghrelin/GHS-R. - Source: PubMed
Publication date: 2025/06/18
Gu MengGe JianchaoXu HuanChen YanboChen QiWang ZhongXu Bin - Ghrelin is a 28 amino acid peptide hormone that impacts a wide range of biological processes, including appetite regulation, glucose metabolism, growth hormone regulation, and cognitive function. To bind and activate its cognate receptor, ghrelin must be acylated on a serine residue in a post-translational modification performed by ghrelin -acyltransferase (GOAT). GOAT is a membrane-bound -acyltransferase (MBOAT) responsible for the catalysis of the addition of an octanoyl fatty acid to the third serine of desacyl ghrelin. Beyond its canonical role for ghrelin maturation in endocrine cells within the stomach, GOAT was recently reported to be overexpressed in prostate cancer (PCa) cells and detected at increased levels in the serum and urine of PCa patients. This suggests GOAT can serve as a potential route for the detection and therapeutic targeting of PCa and other diseases that exhibit GOAT overexpression. Building upon a ghrelin mimetic peptide with nanomolar affinity for GOAT, we developed an antibody-conjugate-inspired system for customizable ligand-conjugate (LC) synthesis allowing for the attachment of a wide range of cargoes. The developed synthetic scheme allows for the easy synthesis of the desired LCs and demonstrates that our ligand system tolerates an extensive palette of cargoes while maintaining nanomolar affinity against GOAT. - Source: PubMed
Publication date: 2025/02/01
Ford Amber LTaft Caine WSprague-Getsy Andrea MCarlson Gracie CMate Nilamber ASieburg Michelle AChisholm John DHougland James L - Whitefish fisheries' side-stream biomass is an abundant underutilized resource that can be valorized to benefit future aquaculture sustainability. Four novel ingredients based on side-streams from Atlantic cod () fileting were produced. FM-hb, a fish meal (FM), and FPH-hb, a fish protein hydrolysate based on heads (h) and backbones (b); FM-hbg, a FM based on heads, backbones, and viscera/guts (g); and FPC-g, a fish protein concentrate based on viscera preserved in formic acid. Four diets were prepared containing one of the ingredients replacing 50% of the dietary FM protein, in addition to a positive (FM10) and a negative (FM5) control. The six diets were fed to triplicate tanks with Atlantic salmon ( L.; 113 ± 1 g) over 8 weeks. Besides general performance, gut and brain gene expression for selected hormones and key neuropeptides involved in the control of appetite and digestive processes were studied during feeding and postprandial, and possible reference levels for Atlantic salmon were established. All side-stream-added diets performed well, with no significant differences in performance and biometrics between the treatments. Some gene expression differences were observed, but no well-defined patterns emerged supporting clear dietary effects related to digestive performance or appetite. However, in the brain, a short-time upregulation of (), corresponded to higher cumulative feed intake (FI) for the FM10 diet supporting notions that this may be a candidate biomarker for appetite in salmon. Expression of stomach () was higher than () and 4 (), and midgut () and () were higher than (). A comparison showed that midgut (), , and expressions were higher than in the hindgut, which is opposite of what is found in mammals. In conclusion, this study shows that sustainable side-stream raw materials with different characteristics can partly replace high-quality commercial FMs giving similar performance. - Source: PubMed
Publication date: 2025/01/30
Sixten Hanne JorunRønnestad IvarBogevik André SAspevik ToneOterhals ÅgeGomes Ana SLai FlorianaTolås IngvillGelebard VirginieHillestad MarieKousoulaki Katerina - Safflower yellow (SY), derived from Carthamus tinctorius L., is a valuable natural edible pigment that exhibits anti-type 2 diabetes mellitus (T2DM) efficacy; however, its mechanism of action is unclear, which hinders its effective use. In this study, we examined the impact of SY on glucose metabolism and insulin secretion both in vivo and in vitro and elucidated the possible underlying mechanism. First, molecular docking demonstrated a strong binding affinity between SY and ghrelin O-acyltransferase (GOAT) protein, which was validated by a cell heat transfer assay (CETSA) and drug affinity response target stability (DARTS) in MIN6 cells. In MIN6 cells, SY increased insulin secretion and showed time- and dose-dependent inhibition of GOAT expression and acyl ghrelin (AG) secretion without affecting the overall levels of ghrelin. Furthermore, ELISA revealed that SY enhanced high glucose (HG)-induced insulin secretion, and immunofluorescence revealed the co-localization of GOAT and ghrelin in MIN6 cells, which was suppressed by SY treatment. The mechanism analysis by Western blot demonstrated that SY downregulated the protein levels of GOAT and GHS-R1a in MIN6 cells while increasing HG-stimulated cAMP and activation of transient receptor potential melastatin 2 (TRPM2). In in vivo experiments, the intraperitoneal injection of SY significantly improved pathological damage to the pancreas, glucose tolerance, and insulin resistance in a mouse model of high-fat diet (HFD)/streptozotocin (STZ)-induced T2DM in a dose-dependent manner. SY enhanced insulin secretion by inhibiting the GOAT/ghrelin system in vivo. In conclusion, we demonstrated that SY exhibits an observable protective effect on diabetes through the GOAT/ghrelin/GHS-R1a/cAMP/TRPM2 pathway. Our findings provide a basis for further investigation of the hypoglycemic mechanism of SY and its potential for further development and utilization. - Source: PubMed
Publication date: 2025/02/11
Ma YunxiaoZhang HaifengYan QihuiWang PingGuo WeiyingYu Lu - LEAP2, a liver-derived antagonist for the ghrelin receptor, GHSR1a, counteracts the effects of ghrelin on appetite and energy balance. Less is known about its impact on blood glucose-regulating hormones from pancreatic islets. Here, we investigate whether acyl-ghrelin (AG) and LEAP2 regulate islet hormone release in a cell-type- and sex-specific manner. Hormone content from secretion experiments with isolated islets from male and female mice was measured by radioimmunoassay and mRNA expression by qPCR. LEAP2 enhanced insulin secretion in islets from males (P < 0.01) but not females (P > 0.2), whilst AG-stimulated somatostatin release was significantly reversed by LEAP2 in males (P < 0.001) but not females (P > 0.2). Glucagon release was not significantly affected by AG and LEAP2. Ghsr1a, Ghrelin, Leap2, Mrap2, Mboat4, and Sstr3 islet mRNA expression did not differ between sexes, whereas the SSTR3 antagonist MK4256 enhanced glucose-induced insulin secretion in islets from males only. In control male islets maintained without 17-beta oestradiol (E2), AG exerted an insulinostatic effect (P < 0.05), with a trend towards reversal by LEAP2 (P = 0.06). Both were abolished by 72 h E2 pre-treatment (10 nmol/L, P > 0.2). AG-stimulated somatostatin release was inhibited by LEAP2 from control (P < 0.001) but not E2-treated islets (P > 0.2). LEAP2 and AG did not modulate insulin secretion from MIN6 beta cells and Mrap2 was downregulated (P < 0.05) and Ghsr1a upregulated (P < 0.0001) in islets from Sst-/- mice. Our findings show that AG and LEAP2 regulate insulin and somatostatin release in an opposing and sex-dependent manner, which in males can be modulated by E2. We suggest that regulation of SST release is a key starting point for understanding the role of GHSR1a in islet function and glucose metabolism. - Source: PubMed
Publication date: 2024/10/28
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