Search results for: FABP3, human recombinant
#33312420 // To Up
Inhibition of vascular adhesion protein-1 modifies hepatic steatosis and .Non-alcoholic fatty liver disease (NAFLD) is associated with obesity, insulin resistance and dyslipidaemia and currently is estimated to affect up to a third of all individuals in developed countries. Current standard of care for patients varies according to disease stage, but includes lifestyle interventions common insulin sensitizers, antioxidants and lipid modifiers. However, to date specific therapies have shown little histological or fibrosis stage improvement in large clinical trials, and there is still no licensed therapy for NAFLD. Given the high prevalence, limited treatment options and significant screening costs for the general population, new treatments are urgently required.
Emma L Shepherd, Sumera Karim, Philip N Newsome, Patricia F Lalor
1072 related Products with: Inhibition of vascular adhesion protein-1 modifies hepatic steatosis and .1000 TESTS/0.65ml100ug100ug Lyophilized100ug Lyophilized100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug 100ul100ug100ug
#32365792 2020/04/30 To Up
Elevated Glucose and Insulin Levels Decrease DHA Transfer across Human Trophoblasts via SIRT1-Dependent Mechanism.Gestational diabetes mellitus (GDM) results in reduced docosahexaenoic acid (DHA) transfer to the fetus, likely due to placental dysfunction. Sirtuin-1 (SIRT1) is a nutrient sensor and regulator of lipid metabolism. This study investigated whether the high glucose and insulin condition of GDM regulates DHA transfer and expression of fatty acid transporters and if this effect is related to SIRT1 expression and function. Syncytialized primary human trophoblasts were treated with and without glucose (25 mmol/L) and insulin (10 mol/L) for 72 h to mimic the insulin-resistance conditions of GDM pregnancies. In control conditions, DHA transfer across trophoblasts increased in a time- and dose-dependent manner. Exposure to GDM conditions significantly decreased DHA transfer, but increased triglyceride accumulation and fatty acid transporter expression (CD36, FABP3, and FABP4). GDM conditions significantly suppressed SIRT1 mRNA and protein expression. The SIRT1 inhibitor decreased DHA transfer across control trophoblasts, and recombinant SIRT1 and SIRT1 activators restored the decreased DHA transport induced by GDM conditions. The results demonstrate a novel role of SIRT1 in the regulation of DHA transfer across trophoblasts. The suppressed SIRT1 expression and the resultant decrease in placental DHA transfer caused by high glucose and insulin levels suggest new insights of molecular mechanisms linking GDM to fetal DHA deficiency.
Jay S Mishra, Hanjie Zhao, Sari Hattis, Sathish Kumar
1001 related Products with: Elevated Glucose and Insulin Levels Decrease DHA Transfer across Human Trophoblasts via SIRT1-Dependent Mechanism.100 ug/vial1 ml100.00 ug50μg/vial1 kit(96 Wells)96 assays20ug250 mg1 ml10μg/vial100 μg500 mg
#31539229 2019/10/11 To Up
Identification of Fatty Acid Binding Protein 5 Inhibitors Through Similarity-Based Screening.Fatty acid binding protein 5 (FABP5) is a promising target for development of inhibitors to help control pain and inflammation. In this work, computer-based docking (DOCK6 program) was employed to screen ∼2 M commercially available compounds to FABP5 based on an X-ray structure complexed with the small molecule inhibitor SBFI-26 previously identified by our group (also through virtual screening). The goal was discovery of additional chemotypes. The screen resulted in the purchase of 78 candidates, which led to the identification of a new inhibitor scaffold (STK-0) with micromolar affinity and apparent selectivity for FABP5 over FABP3. A second similarity-based screen resulted in three additional hits (STK-15, STK-21, STK-22) from which preliminary SAR could be derived. Notably, STK-15 showed comparable activity to the SBFI-26 reference under the same assay conditions (1.40 vs 0.86 μM). Additional molecular dynamics simulations, free energy calculations, and structural analysis (starting from DOCK-generated poses) revealed that R enantiomers (dihydropyrrole scaffold) of STK-15 and STK-22 have a more optimal composition of functional groups to facilitate additional H-bonds with Arg109 of FABP5. This observation suggests enantiomerically pure compounds could show enhanced activity. Overall, our study highlights the utility of using similarity-based screening methods to discover new inhibitor chemotypes, and the identified FABP5 hits provide a strong starting point for future efforts geared to improve activity.
Yuchen Zhou, Matthew W Elmes, Joseph M Sweeney, Olivia M Joseph, Joyce Che, Hao-Chi Hsu, Huilin Li, Dale G Deutsch, Iwao Ojima, Martin Kaczocha, Robert C Rizzo
2811 related Products with: Identification of Fatty Acid Binding Protein 5 Inhibitors Through Similarity-Based Screening.1 mg96tests50gm100tests50ul400Tests500g500gm5X100Ul25 mg
#26601584 2015/11/18 To Up
Overexpression of SREBP1 (sterol regulatory element binding protein 1) promotes de novo fatty acid synthesis and triacylglycerol accumulation in goat mammary epithelial cells.Sterol regulatory element binding protein 1 (SREBP1; gene name SREBF1) is known to be the master regulator of lipid homeostasis in mammals, including milk fat synthesis. The major role of SREBP1 in controlling milk fat synthesis has been demonstrated in bovine mammary epithelial cells. Except for a demonstrated role in controlling the expression of FASN, a regulatory role of SREBP1 on milk fat synthesis is very likely, but has not yet been demonstrated in goat mammary epithelial cells (GMEC). To explore the regulatory function of SREBP1 on de novo fatty acids and triacylglycerol synthesis in GMEC, we overexpressed the mature form of SREBP1 (active NH2-terminal fragment) in GMEC using a recombinant adenovirus vector (Ad-nSREBP1), with Ad-GFP (recombinant adenovirus of green fluorescent protein) as control, and infected the GMEC for 48 h. In infected cells, we assessed the expression of 20 genes related to milk fat synthesis using real time-quantitative PCR, the protein abundance of SREBP1 and FASN by Western blot, the production of triacylglycerol, and the fatty acid profile. Expression of SREBF1 was modest in mammary compared with the other tissues in dairy goats but its expression increased approximately 30-fold from pregnancy to lactation. The overexpression of the mature form of SREBP1 was confirmed by >200-fold higher expression of SREBF1 in Ad-nSREBP1 compared with Ad-GFP. We observed no changes in amount of the precursor form of SREBP1 protein but a >10-fold increase of the mature form of SREBP1 protein with Ad-nSREBP1. Compared with Ad-GFP cells (control), Ad-nSREBP1 cells had a significant increase in expression of genes related to long-chain fatty acid activation (ACSL1), transport (FABP3), desaturation (SCD1), de novo synthesis of fatty acids (ACSS2, ACLY, IDH1, ACACA, FASN, and ELOVL6), and transcriptional factors (NR1H3 and PPARG). We observed a >10-fold increase in expression of INSIG1 but SCAP was downregulated by Ad-nSREBP1. Among genes related to milk fat synthesis and lipid droplet formation, only LPIN1 and DGAT1 were upregulated by Ad-nSREBP1. Compared with the Ad-GFP, the cellular triacylglycerol content was higher and the percentage of C16:0 and C18:1 increased, whereas that of C16:1, C18:0, and C18:2 decreased in Ad-nSREBP1 cells. Overall, the data provide strong support for a central role of SREBP1 in the regulation of milk fat synthesis in goat mammary cells.
H F Xu, J Luo, W S Zhao, Y C Yang, H B Tian, H B Shi, M Bionaz
1441 related Products with: Overexpression of SREBP1 (sterol regulatory element binding protein 1) promotes de novo fatty acid synthesis and triacylglycerol accumulation in goat mammary epithelial cells.96tests1 mg100 μg100 μg100ug Lyophilized100 μg100ug Lyophilized100.00 ug100ug Lyophilized100 ul
#23113681 2012/11/01 To Up
Clinical and analytical evaluation of an immunoturbidimetric heart-type fatty acid-binding protein assay.Heart-type fatty acid-binding protein (H-FABP) is a low molecular weight protein involved in the intracellular uptake and buffering of long chain fatty acids in the myocardium. It is an early marker for ACS. We have evaluated the Randox Laboratories immunoturbidimetric assay on a Siemens Advia 1800 analyzer. The assay employs latex particles coated with mouse monoclonal anti-HFABP antibodies to generate turbidity.
Daniel R Carless, Małgorzata Wnęk, Catherine Knox, Kevin R Harrison, Nicola Calder, Alistair S Hall, Julian H Barth
1820 related Products with: Clinical and analytical evaluation of an immunoturbidimetric heart-type fatty acid-binding protein assay.1 mg1000 TESTS/0.65ml96tests1 kit0.1 mg
#20696127 2010/08/07 To Up
Highly sensitive recombinant antibodies capable of reliably differentiating heart-type fatty acid binding protein from noncardiac isoforms.During recent times, heart-type fatty acid binding protein (hFABP) has gained increasing credence as a promising cardiac biomarker. This is largely due to its rapid myocardial release and subsequent clearance kinetics, which are superior to those of myoglobin and offer an earlier diagnostic window than the troponins. Realization of its full diagnostic and prognostic potential is dependent on accessibility to robust hFABP-specific assays. Here we describe a rational strategy for generation and screening of hFABP-specific avian-derived recombinant antibodies. These antibodies were confirmed to be exquisitely specific for hFABP, with no cross-reactivity observed in a representative panel of the most homologous non-heart-type FABP isoforms. All of the antibodies tested exhibited single-figure nanomolar affinities, and their analytical potential was demonstrated in a simple inhibition enzyme-linked immunosorbent assay (ELISA) format that returned an impressive limit of quantitation (LOQ) value of 1.9 ng/ml. The cumulative results underline the potential value of these antibodies as enabling reagents for use in a variety of immunodiagnostic configurations.
B Vijayalakshmi Ayyar, Stephen Hearty, Richard O'Kennedy
1948 related Products with: Highly sensitive recombinant antibodies capable of reliably differentiating heart-type fatty acid binding protein from noncardiac isoforms.1 mg96tests500.2 mg2 Pieces/Box10500100 100 ug100.00 ug1mg50
#19564161 2009/06/29 To Up
Serum 99th centile values for two heart-type fatty acid binding protein assays.We have previously demonstrated that heart-type fatty acid binding protein (H-FABP) is an independent prognostic marker for survival after acute coronary syndrome (ACS). This study aimed to define the 99th centile values for H-FABP as determined with two different assays, and to study the relationship with age, gender and renal function.
D P Bathia, D R Carless, K Viswanathan, A S Hall, J H Barth
2291 related Products with: Serum 99th centile values for two heart-type fatty acid binding protein assays.96tests1 mg96T1x96 well plate96T96T100 assays96T0.1 mg96T
#12479569 // To Up
Solution structure of fatty acid-binding protein from human brain.Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting often antiparallel beta-strands (betaA to betaJ) that form two almost orthogonal beta-sheets, a helix-turn-helix motif that closes the beta-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity.
Martin Rademacher, Aukje W Zimmerman, Heinz Rüterjans, Jacques H Veerkamp, Christian Lücke96tests1 mg 100ul100 μg1 mg20 μg50ul 100ul 100ul 100ul1 kit(96 Wells) 100ul
#11478368 // To Up
Fatty acid-binding proteins of nervous tissue.Fatty acid-binding proteins (FABPs) are cytosolic 14-15 kDa proteins, which are supposed to be involved in fatty acid (FA) uptake, transport, and targeting. They may modulate FA concentration and in this way influence function of enzymes, membranes, ion channels and receptors, and gene expression and cellular growth and differentiation. Nine FABP types can be discerned with a specific tissue distribution. In spite of 30-70% amino acid sequence identity, they have a similar tertiary, beta-clam structure in which the FA is bound. Nervous tissue contains four FABP types with a distinct spatio-temporal distribution. Myelin (M)-FABP is only present in the peripheral nerves, brain (B)-FABP and epidermal (E)-FABP mainly in glial cells and neurons, respectively of pre- and perinatal brain, and heart (H)-FABP in adult brain. Possible functions of FABPs in the nervous system are discussed. Binding studies with a range of physiological FA showed no large differences between recombinant proteins of the four human FABP types in binding specificity and affinity, also not for polyunsaturated FA (PUFA). The transfer of FA from fixed liposomes to mitochondria was similarly promoted by the four types. A marked difference in conformational stability was observed with H-FABP > B-FABP > M-FABP > E-FABP. Surface epitopes of H-FABP showed reaction with anti-B-FABP antibodies, but no other cross-reactivity of FABP type and heterologous antibodies was observed. The functional significance of the distinct spatio-temporal pattern of the four FABP types remains to be elucidated.
J H Veerkamp, A W Zimmerman1 mg96tests1 mg500g100tests50gm100ug100g 100 UG
#10854433 // To Up
Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein.Expression of brain fatty acid-binding protein (B-FABP) is spatially and temporally correlated with neuronal differentiation during brain development. Isothermal titration calorimetry demonstrates that recombinant human B-FABP clearly exhibits high affinity for the polyunsaturated n-3 fatty acids alpha-linolenic acid, eicosapentaenoic acid, docosahexaenoic acid, and for monounsaturated n-9 oleic acid (K(d) from 28 to 53 nm) over polyunsaturated n-6 fatty acids, linoleic acid, and arachidonic acid (K(d) from 115 to 206 nm). B-FABP has low binding affinity for saturated long chain fatty acids. The three-dimensional structure of recombinant human B-FABP in complex with oleic acid shows that the oleic acid hydrocarbon tail assumes a "U-shaped" conformation, whereas in the complex with docosahexaenoic acid the hydrocarbon tail adopts a helical conformation. A comparison of the three-dimensional structures and binding properties of human B-FABP with other homologous FABPs, indicates that the binding specificity is in part the result of nonconserved amino acid Phe(104), which interacts with double bonds present in the lipid hydrocarbon tail. In this context, analysis of the primary and tertiary structures of human B-FABP provides a rationale for its high affinity and specificity for polyunsaturated fatty acids. The expression of B-FABP in glial cells and its high affinity for docosahexaenoic acid, which is known to be an important component of neuronal membranes, points toward a role for B-FABP in supplying brain abundant fatty acids to the developing neuron.
G K Balendiran, F Schnutgen, G Scapin, T Borchers, N Xhong, K Lim, R Godbout, F Spener, J C Sacchettini
2887 related Products with: Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein.96tests1 mg1 mg 100ul100 μg 100ul 100ul0.1 mg1 kit(96 Wells)96T 100ul20 μg
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