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anti-Human FABP1 Antikörper:
anti-Mouse (Murine) FABP1 Antikörper:
anti-Rat (Rattus) FABP1 Antikörper:
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Human Polyclonal FABP1 Primary Antibody für ICC, IF - ABIN4309903
Yan, Janda, Chang, Zheng, Larkin, Luca, Chia, Mah, Han, Terry, Ootani, Roelf, Lee, Yuan, Li, Bolen, Wilhelmy, Davies, Ueno, von Furstenberg, Belgrader, Ziraldo, Ordonez, Henning, Wong, Snyder et al.: Non-equivalence of Wnt and R-spondin ligands during Lgr5(+) intestinal stem-cell self-renewal. ... in Nature 2017
Show all 2 Pubmed References
Human Monoclonal FABP1 Primary Antibody für IA, FACS - ABIN2191917
Bax, Siersema, Haringsma, Kuipers, Vos, Van Dekken, Van Vliet, Kusters: High-grade dysplasia in Barrett's esophagus is associated with increased expression of calgranulin A and B. in Scandinavian journal of gastroenterology 2007
This study demonstrated that the loss of FABP1 expression is associated with MSI (zeige MSI1 Antikörper) carcinomas and that interferon gamma (zeige IFNG Antikörper) stimulation plays a role in this process via its interaction with PPARgamma (zeige PPARG Antikörper).
Hepatic adenomas co-occurring with fibrolamellar carcinomas show LFABP loss and are negative for PRKACA (zeige PRKACA Antikörper) rearrangements, indicating they are genetically distinct lesions. These data also demonstrate that LFABP loss, which characterizes HNF1-alpha (zeige HNF1A Antikörper) inactivation, is a consistent feature of fibrolamellar carcinoma, indicating HNF1-alpha (zeige HNF1A Antikörper) inactivation is an important event in fibrolamellar carcinoma pathogenesis.
studies indicate that FABP1 is essential for proper lipid metabolism in differentiated enterocytes, particularly concerning fatty acids uptake and its basolateral secretion.
CDH5 (zeige CDH5 Antikörper) and FABP1 expression levels were both elevated in drug-induced liver injury.
A high resolution NMR comparative molecular analysis of L-FABP T94T and L-FABP T94A in their unbound states and in the presence of representative ligands of the fatty acid and bile acid classes showed that threonine to alanine replacement did not result in strongly perturbed structural and dynamic features, although differences in oleic acid binding by the two variants were detected.
Studies show that despite overall tertiary structure similarity, the hFABP1 differs significantly from rat FABP1 in secondary structure, much larger ligand binding cavity, and affinities/specificities for some ligands. Moreover, while both mouse and hFABP1 mediate ligand induction of PPARA (zeige PPARA Antikörper), they differ markedly in genes induced. hFABP1 T94A variant is associated with altered body mass index.[review]
Urinary L-FABP, NGAL (zeige LCN2 Antikörper), Kim-1 (zeige HAVCR1 Antikörper) and albumin (zeige ALB Antikörper) levels increased during the acute phase of kidney injury and were significantly correlated with the degree of tubulointerstitial fibrosis during the chronic phase. These markers could detect higher risk of progression to CKD.
L-FABP was found to associate with VEGFR2 on membrane rafts and subsequently activate the Akt/mTOR/P70S6K/4EBP1 and Src/FAK/cdc42 pathways, which resulted in up-regulation of VEGF-A accompanied by an increase in both angiogenic potential and migration activity. L-FABP significantly promoted tumor growth and metastasis in a xenograft mouse model.
In chronic kidney disease, high urinary L-FABP correlated with the development of end-stage renal disease and cardiovascular disease.
In the association of SNPs in FABP1 gene with PCOS, rs2197076 was more closely associated with its main features than rs2241883 and seemed to play a more important role in the pathogenesis of PCOS.
Thermal aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has been studied at various temperatures and various protein concentrations by dynamic light scattering.
role of Fabp1/Scp-2 (zeige CRISP3 Antikörper) in hepatic phytol metabolism
Individually ablating SCPx (zeige SCP2 Antikörper) or SCP2/SCPx (zeige SCP2 Antikörper) elicited concomitant upregulation of L-FABP.
Lack of a significant decrease in the flux of HDL-[(3)H]CE to biliary FC or bile acids in FABP1(-/-) mice indicates the likely compensation of its function by an as yet unidentified mechanism. Taken together, these studies demonstrate that FABP1 and SCP2 facilitate the preferential movement of HDL-CEs to bile for final elimination
data showed that Fabp1 gene ablation markedly diminished the impact of high-fat diet on brain endocannabinoid levels, especially in male mice
Studies show that despite overall tertiary structure similarity, the hFABP1 differs significantly from rat FABP1 in secondary structure, much larger ligand binding cavity, and affinities/specificities for some ligands. Moreover, while both mouse and hFABP1 mediate ligand induction of PPARA (zeige PPARA Antikörper), they differ markedly in genes induced.
FABP1 knockout increased brain levels of arachidonic acid-containing endocannabinoids
L-FABP was more important in hepatic retention of bile acids, while SCP-2/SCP-x (zeige SCP2 Antikörper) more broadly affected biliary bile acid and phospholipid levels.
These findings suggest that some of the phenotypic divergence between the two L-Fabp(-/-) lines may reflect unanticipated differences in genetic background, underscoring the importance of genetic background in phenotypic characterization.
Loss of L-FABP and SCP-2 (zeige CRISP3 Antikörper), or both induces hepatic lipid accumulation in female mice and mimics non-alcoholic fatty liver disease.
L-FABP appears to function more in hepatic retention of bile acids as well as hepatic uptake and biliary secretion of HDL (zeige HSD11B1 Antikörper)-cholesterol
combinatorial interactions between multiple regulatory factors are responsible for the gene expression of L-FABP in the liver
This gene encodes the fatty acid binding protein found in liver. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. This protein and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism.
fatty acid-binding protein 1
, fatty acid-binding protein, liver
, liver-type fatty acid-binding protein
, aspartate aminotransferase, mitochondrial
, fatty acid-binding protein
, glutamate oxaloacetate transaminase 2
, kynurenine aminotransferase 4
, kynurenine aminotransferase IV
, kynurenine--oxoglutarate transaminase 4
, kynurenine--oxoglutarate transaminase IV
, plasma membrane-associated fatty acid-binding protein
, transaminase A
, aspartate aminotransferase 2
, 14 kDa selenium-binding protein
, fatty acid binding protein liver
, squalene- and sterol-carrier protein
, fatty acid binding protein 1, liver
, fafatty acid binding protein 1, liver
, liver fatty acid binding protein
, fatty acid binding protein 1-A, liver
, LOW QUALITY PROTEIN: fatty acid-binding protein, liver
, Aspartate aminotransferase, mitochondrial
, Fatty acid-binding protein
, Glutamate oxaloacetate transaminase 2
, Kynurenine aminotransferase 4
, Kynurenine aminotransferase IV
, Kynurenine--oxoglutarate transaminase 4
, Kynurenine--oxoglutarate transaminase IV
, Plasma membrane-associated fatty acid-binding protein
, Transaminase A
, glutamic-oxaloacetic transaminase 2, mitochondrial