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anti-Mouse (Murine) ANGPTL4 Antibodies:
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Human Polyclonal ANGPTL4 Primary Antibody for ELISA, WB - ABIN565533
Yokouchi, Eto, Nishimura, Takeda, Kaburagi, Yamamoto, Yasuda: Angiopoietin-like protein 4 (ANGPTL4) is induced by high glucose in retinal pigment epithelial cells and exhibits potent angiogenic activity on retinal endothelial cells. in Acta ophthalmologica 2013
Human Polyclonal ANGPTL4 Primary Antibody for WB - ABIN526478
Makoveichuk, Sukonina, Kroupa, Thulin, Ehrenborg, Olivecrona, Olivecrona: Inactivation of lipoprotein lipase occurs on the surface of THP-1 macrophages where oligomers of angiopoietin-like protein 4 are formed. in Biochemical and biophysical research communications 2012
Human Polyclonal ANGPTL4 Primary Antibody for ELISA, WB - ABIN1169313
Broxmeyer, Srour, Cooper, Wallace, Hangoc, Youn: Angiopoietin-like-2 and -3 act through their coiled-coil domains to enhance survival and replating capacity of human cord blood hematopoietic progenitors. in Blood cells, molecules & diseases 2012
Human Polyclonal ANGPTL4 Primary Antibody for FACS, IHC (p) - ABIN653155
Wan, Wen, Dong, Tang, Liu, Liu, Tao, Gao, Sun, Cao, Fan, Wu: Establishment of monoclonal HCC cell lines with organ site-specific tropisms. in BMC cancer 2015
increase in angiopoietin-like protein 4 messenger RNA across multiple models of altered energy balance identifies it as an adipokine that is uniquely responsive to changes in energy balance in the lactating dairy cow
These findings indicate that liver and adipose tissue are key sources of ANGPTL4 in cattle; the protein was also highly abundant in ruminal epithelium, making it possible that commensal microbes may influence ANGPTL4 synthesis and secretion.
1) ANGPTL4 is not involved in the triglyceride-lowering effect ofbile acids ; 2) ANGPTL4 promotes bile acids absorption during taurocholic acid supplementation via a mechanism dependent on the gut (show GUSB Antibodies) microbiota.
physiological changes in adipose tissue ANGPTL4 expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL (show LPL Antibodies) in wild-type mice, but not Angptl4(-/-) mice. We conclude that ANGPTL4 promotes loss of intracellular LPL (show LPL Antibodies) by stimulating LPL (show LPL Antibodies) degradation after LPL (show LPL Antibodies) processing in the endoplasmic reticulum (ER).
This study shows that TNF-alpha (show TNF Antibodies), by a Foxo1 (show FOXO1 Antibodies) dependent pathway, increases the transcription of ANGPTL4 which is secreted by the cells and causes inactivation of LPL (show LPL Antibodies).
Angptl4-deficient mice show impaired insulin (show INS Antibodies) secretion and dysmorphic pancreatic islets.
Angptl4 induces obesity-associated metabolic disorders. The present study suggested that Angptl4 promotes liver steatosis and lipolysis, in addition to impairing liver function; while Angptl4 improves glucose tolerance and insulin (show INS Antibodies) resistance, in addition to causing the downregulation of various insulin (show INS Antibodies) signaling pathway-associated genes.
ANGPTL4 is part of a shuttling mechanism that directs fatty acids derived from circulating triglyceride-rich lipoproteins to brown adipose tissue during cold.
This model suggests a general mechanism by which TAG trafficking is coordinated by lipasin, Angptl3 (show ANGPTL3 Antibodies) and Angptl4 at different nutritional statuses.
These results reveal that FTO (show FTO Antibodies) regulates fatty acid mobilization in adipocytes and thus body weight in part through posttranscriptional regulation of Angptl4.
these results suggest that IL-1beta (show IL1B Antibodies) increases Angptl4 expression through a mechanism dependent on the JNK (show MAPK8 Antibodies)-MAPK (show MAPK1 Antibodies) signaling pathway in MC3T3-E1 cells.
glucagon receptor (show GCGR Antibodies) antagonist improves glycemia in diet-induced obese angptl4 knockout mice without increasing glucagon (show GCG Antibodies) levels or alpha-cell proliferation, underscoring the importance of this protein.
These results suggested that ANGPTL4 was essential for proliferation and metastasis of lung cancer cells.
The mutant tumors exhibited impaired proliferation, anoikis resistance, and migratory capability and had reduced adenylate energy charge. Further investigations also revealed that cANGPTL4 regulated the expression of Glut2 (show SLC2A2 Antibodies)
Data indicate angiopoietin-like 4 (ANGPTL4) as a key player that coordinates an increase in cellular energy flux crucial for EMT (show ITK Antibodies) via an ANGPTL4/14-3-3gamma (show YWHAG Antibodies) signaling axis.
The authors now show: (1) that ANGPTL4 inactivates LPL (show LCP1 Antibodies) by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 (show GPIHBP1 Antibodies) renders LPL (show LCP1 Antibodies) largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 (show GPIHBP1 Antibodies) are required for this protective effect.
One of the variants, rs116843064, is a damaging missense variant within the ANGPTL4 gene.
reduced expression of one of the survival-associated transcripts, Angiopoietin-like 4, impairs growth of a gemcitabine-resistant pancreatic cancer cell line.
Serum ANGPTL4 is elevated in coronary artery disease, but levels do not reflect severity of disease.
identify ANGPTL4 as a Wnt (show WNT2 Antibodies) signaling antagonist that binds to syndecans and forms a ternary complex with the Wnt (show WNT2 Antibodies) co-receptor Lipoprotein receptor-related protein 6 (show LRP6 Antibodies)
results suggest that ANGPTL4 could contribute to the development of retinal neovascularization in sickle cell patients and could therefore be a therapeutic target for the treatment of PSR (show JMJD6 Antibodies)
Data suggest that purified FLD (show LPIN1 Antibodies) (C-terminal fibrinogen-like domain) of ANGPTL4 is sufficient to stimulate lipolysis in primary adipocytes; increasing circulating FLD (show LPIN1 Antibodies) levels in mice not only induces white adipose tissue lipolysis in vivo but also reduces diet-induced obesity without affecting LPL (lipoprotein lipase (show LPL Antibodies)) activity; increasing systemic FLD (show LPIN1 Antibodies) levels induces beige (show LYST Antibodies) conversion in white adipose tissue.
The ANGPTL4 G/A polymerase chain reaction-single strand conformation polymorphism (PCR-SSCP) showed a significant effect on intramuscular fat
These results suggest that the microbiota might regulate host intestinal Angptl4 protein expression and peripheral fat storage by suppressing the activity of an intestine-specific transcriptional enhancer.
This gene is a member of the angiopoietin/angiopoietin-like gene family and encodes a glycosylated, secreted protein with a fibrinogen C-terminal domain. This gene is induced under hypoxic conditions in endothelial cells and is the target of peroxisome proliferation activators. The encoded protein is a serum hormone directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity and also acts as an apoptosis survival factor for vascular endothelial cells. The encoded protein may play a role in several cancers and it also has been shown to prevent the metastatic process by inhibiting vascular activity as well as tumor cell motility and invasiveness. Decreased expression of this protein has been associated with type 2 diabetes. Alternatively spliced transcript variants encoding different isoforms have been described. This gene was previously referred to as ANGPTL2 but has been renamed ANGPTL4.
, Angiopoietin-related protein 4
, angiopoietin-related protein 4-like
, angiopoietin-like protein 4
, angiopoietin-related protein 4
, fasting-induced adipose factor
, fibrinogen/angiopoietin-related protein
, hepatic fibrinogen/angiopoietin-related protein
, major histocompatibility complex region NG27
, secreted protein Bk89
, PPARG angiopoietin related protein
, hepatic angiopoietin-related protein
, peroxisome proliferator-activated receptor (PPAR) gamma induced angiopoietin-related protein
, PPARG angiopoietin-related protein
, angiopoietin-like secreted glycoprotein 4
, angiopoietin-like 4 protein