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Angiopoietin-like protein 4 (ANGPTL4) ELISA Kit
Fasting-induced adipose factor (FIAF) ELISA Kit

Lipoprotein lipase and angiopoietin-like 4 - Cardiomyocyte secretory proteins that regulate metabolism during diabetic heart disease

Abstract Cardiac diseases have been extensively studied following diabetes and altered metabolism has been implicated in its initiation. In this context, there is a shift from glucose utilization to predominantly fatty acid metabolism. We have focused on the micro- and macro-environments that the heart uses to provide fatty acids to the cardiomyocyte. Specifically, we will discuss the cross talk between endothelial cells, smooth muscles and cardiomyocytes, and their respective secretory products that allows for this shift in metabolism. These changes will then be linked to alterations in the cardiovascular system and the augmented heart disease observed during diabetes. Traditionally, the heart was only thought of as an organ that supplies oxygen and nutrients to the body through its function as a pump. However, the heart as an endocrine organ has also been suggested.Secreted products from the cardiomyocytes include the natriuretic peptides atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). Both have been shown to have vasodilatory, diuretic and antihypertensive effects. These peptides have been extensively studied and their deficiency is considered to be a major cause for the initiation of cardiovascular and cardiometabolic disorders. Another secretory enzyme, lipoprotein lipase (LPL), has been implicated in diabetic heart disease. LPL is a triglyceride-hydrolyzing enzyme that is synthesized within the cardiomyocyte and secretedtowards the lumen under various conditions. For example, moderate or short-term hyperglycemia stimulates the release of LPL from the cardiomyocytes towards the endothelial cells. This process allows LPL to contact lipoprotein triglycerides, initiating their break down, with the product of lipolysis (free fatty acids, FA) translocating towards the cardiomyocytes for energy consumption. This mechanism compensates for the lack of glucose availability following diabetes. Under prolonged, chronic conditions of hyperglycemia, there is a need to inhibit this mechanism to avoid the excess delivery of FA to the cardiomyocytes, an effect that is known to induce cardiac cell death. Thus, LPL inhibition is made possible by a FA-induced activation of PPAR β/δ, which augments angiopoietin-like 4 (Angptl4), an inhibitor of LPL activity. In the current review, we will focus on the mediators and conditions that regulate LPL and Angptl4 secretion from the cardiomyocyte, which are critical for maintaining cardiac metabolic homeostasis.
Puthanveetil P, Wan A, Rodrigues B. Crit Rev Clin Lab Sci. 2015 Jan 19:1-12. [Epub ahead of print]

Angptl4 serves as an endogenous inhibitor of intestinal lipid digestion

Dietary triglycerides are hydrolyzed in the small intestine principally by pancreatic lipase. Following uptake by enterocytes and secretion as chylomicrons, dietary lipids are cleared from the bloodstream via lipoprotein lipase. Whereas lipoprotein lipase is inhibited by several proteins including Angiopoietin-like 4 (Angptl4), no endogenous regulator of pancreatic lipase has yet been identified. Here we present evidence that Angptl4 is an endogenous inhibitor of dietary lipid digestion. Angptl4-/- mice were heavier compared to their wild-type counterparts without any difference in food intake, energy expenditure or locomotor activity. However, Angptl4-/- mice showed decreased lipid content in the stools and increased accumulation of dietary triglycerides in the small intestine, which coincided with elevated luminal lipase activity in Angptl4-/- mice. Furthermore, recombinant Angptl4 reduced the activity of pancreatic lipase as well as the lipase activity in human ileostomy output. In conclusion, our data suggest that Angptl4 is an endogenous inhibitor of intestinal lipase activity.
Mattijssen F et al. Mol Metab. 2013 Nov 20;3(2):135-44

Skeletal Actions of Fasting-Induced Adipose Factor (FIAF)

Several adipokines are known to influence skeletal metabolism. Fasting-induced adipose factor (FIAF) is an adipokine that gives rise to 2 further peptides in vivo, the N-terminal coiled-coil domain (FIAFCCD) and C-terminal fibrinogen-like domain (FIAFFLD). The skeletal action of these peptides is still uncertain. Our results show that FIAFCCD is a potent inhibitor of osteoclastogenesis and function, as seen in mouse bone marrow and RAW264.7 cell cultures, and in a resorption assay using isolated primary mature osteoclasts. The inhibitory effects at 500 ng/mL were approximately 90%, 50% and 90%, respectively, in these assays. FIAFCCD also stimulated osteoblast mitogenesis by approximately 30% at this concentration. In comparison, FIAFFLD was only active in decreasing osteoblast mitogenesis, and intact FIAF had no effect in any of these assays. In murine bone marrow cultures, FIAFCCD reduced the expression of macrophage colony-stimulating factor (M-CSF), nuclear factor of activated T-cells c1 (NFATc1) and dendritic cell-specific transmembrane protein (DC-STAMP), and to lesser extent suppressed the expression of connective tissue growth factor (CTGF). FIAFCCD also decreased expression of M-CSF and CTGF in stromal/osteoblastic ST2 cells. Its effect on receptor activator of nuclear factor κB (RANKL) and osteoprotegerin expression in bone marrow was not consistent with its inhibitory action on osteoclastogenesis, but it decreased RANKL expression in ST2 cells. In RAW264.7 cell cultures, FIAFCCD significantly reduced the expression of NFATc1 and DC-STAMP. In conclusion, FIAFCCDinhibits osteoclast differentiation and function in vitro and decreases expression of genes encoding key osteoclastogenic factors such as M-CSF, CTGF, NFATc1, and DC-STAMP. FIAFCCD's action on osteoclasts may be independent of the RANKL/osteoprotegerin pathway. These results suggest a novel mechanism by which adipose tissue may regulate bone resorption and skeletal health.
Jian-ming Lin, et al. Endocrinology en.2013-1238
MicroRNAs (miRNAs) as modulators of gene expression have been described to display both tumor-promoting and tumor-suppressive functions. Although their role has been studied in different tumor types, little is known about how they regulate nuclear factor κB (NF-κB) signaling in breast cancer. Here, we performed an unbiased whole genome miRNA (miRome) screen to identify novel modulators of NF-κB pathway in breast cancer. The screen identified 13 miRNA families whose members induced consistent effects on NF-κB activity. Among those, the miR-520/373 family inhibited NF-κB signaling through direct targeting of RELA and thus strongly reduced expression and secretion of the pro-inflammatory cytokines interleukin (IL)-6 and IL-8. With a combination of in vitro and in vivo approaches, we propose a metastasis-suppressive role of miR-520/373 family. miR-520c and miR-373 abrogated both in vitro cell invasion and in vivo intravasation of highly invasive MDA-MB-231 cells. However, knockdown of RELA did not affect their metastatic ability. mRNA profiling of MDA-MB-231 cells on overexpression of miR-520/373 members revealed a strong downregulation of transforming growth factor-β (TGF-β) signaling. Mechanistically, the metastasis-suppressive role of miR-520/373 can be attributed to direct suppression of TGFBR2, as the silencing of TGFBR2 phenocopied the effects of miR-520/373 overexpression on suppression of Smad-dependent expression of the metastasis-promoting genes parathyroid hormone-related protein, plasminogen activator inhibitor-1 and angiopoietin-like 4 as well as tumor cell invasion, in vitro and in vivo. A negative correlation between miR-520c and TGFBR2 expression was observed in estrogen receptor negative (ER(-)) breast cancer patients but not in the ER positive (ER(+)) subtype. Remarkably, decreased expression of miR-520c correlated with lymph node metastasis specifically in ER(-) tumors. Taken together, our findings reveal that miR-520/373 family has a tumor-suppressive role in ER(-) breast cancer by acting as a link between the NF-κB and TGF-β pathways and may thus contribute to the interplay of tumor progression, metastasis and inflammation.
Keklikoglou I et al. Oncogene. 2012 Sep 13;31(37):4150-63
Purpose:  Hyperglycaemia has been identified as major risk factor for diabetic retinopathy (DR). It is widely accepted that the progression of DR is mainly due to a local imbalance of pro- versus anti-angiogenic factors in the retina. In this study, we investigated whether retinal pigment epithelial (RPE) cells produced pro-angiogenic factors under high glucose (HG) conditions in vitro. Methods:  Cultured human retinal endothelial (RE) cells were exposed to conditioned medium from retinal pigment epithelium cells (ARPE-19) grown in HG medium and assessed for tube formation. Based on the expression profiles of ARPE-19, we investigated whether ANGPTL4 was a major angiogenic factor released from ARPE-19 under HG conditions using cultured human RE cells as the test system for experiments with recombinant protein, conditioned medium from ARPE-19 and RNA interference (RNAi). Results:  The conditioned medium from ARPE-19 cultured under HG conditions promoted tube formation of cultured human RE cells. GeneChip analysis showed that ANGPTL4 was one of the highest upregulated genes under HG conditions. In addition, recombinant ANGPTL4promoted all of the elements of angiogenesis in human RE cells in vitro. The results of experiments using conditioned medium from ARPE-19 combined with RNAi demonstrated that ANGPTL4 was a major angiogenic factor released from ARPE-19 under HG conditions. Conclusions: ANGPTL4 was induced by high glucose in RPE cells and exhibited potent angiogenic activity on RE cells. Our results are unique and may potentially add a new candidate to the long list of molecules involved in diabetic retinopathy.
Yokouchi H et al. Acta Ophthalmol. 2013 Feb 7. doi: 10.1111/aos.12097. [Epub ahead of print]

Hypothalamic Angptl4/Fiaf Is a Novel Regulator of Food Intake and Body Weight

OBJECTIVE The angiopoietin-like protein 4 (Angptl4)/fasting-induced adipose factor (Fiaf) is known as a regulator of peripheral lipid and glucose metabolism. In the present study, we investigated the physiological role of Angptl4 in central regulation of body weight homeostasis.
RESEARCH DESIGN AND METHODS Hypothalamic Angptl4 expression levels were measured using immunoblot assay during feeding manipulation or after administration of leptin, insulin, and nutrients. The effects of Angptl4 on food intake, body weight, and energy expenditure were determined following intracerebroventricular (ICV) administration of Angptl4 in C57BL/6 mice. Food intake, energy metabolism, and feeding responses to leptin, insulin, and nutrients were compared between Angptl4-null mice and their wild littermates. Finally, the relationship of hypothalamic AMP-activated protein kinase (AMPK) and Angptl4 was studied.
RESULTS Hypothalamic Angptl4 expression levels were increased upon food intake or administration of leptin, insulin, and nutrients. Furthermore, central administration of Angptl4 suppressed food intake and body weight gain but enhanced energy expenditure. These effects were mediated via suppression of hypothalamic AMPK activities. Consistently, Angptl4-null mice displayed increased body weight and hypothalamic AMPK activity but reduced energy expenditure. Food intake following a fast was significantly greater in Angptl4-null mice, which was normalized by centrally administered Angptl4. Moreover, anorectic responses to leptin, insulin, and glucose were diminished in Angptl4-null mice. In contrast, Angptl4-null mice were resistant to diet-induced obesity, indicating obesity-promoting effects of Angptl4 under the condition of fat-enriched diet.
CONCLUSIONS We have demonstrated that hypothalamic Angptl4 is regulated by physiological appetite regulators and mediates their anorexigenic effects via inhibition of hypothalamic AMPK activity. Therefore, Angptl4 appears to have an important role in central regulation of energy metabolism.
Kim HK, et al. Diabetes vol. 59 no. 11 2772-2780
human angptl4
mouse angptl4 recombinant
rat angptl4
anti angptl4 antibody for immunohistochemistry a00390-02-100 from aviscera bioscience

Human ANGPTL-4 ELISA Kit had been used by following research paper

Supplementary Information (doc 144K) - Nature

angptl4 (Human) elisa kit SK00309-01 from aviscera bioscience Human ANGPTL4 ELISA Kit
Code No.: SK00309-01
Size: 96 T
Price: $360.00
Standard range 0.312-40 ng/ml
Sensitivity: 0.15 ng/ml
Sample Type:serum, plasma
Dilution Factor: 4
Sample require: 100 ul per well
Intra-CV: 4-6 %
Inter-CV: 8-10%
Data Sheet: PDF
anti angptl4 antibody Anti ANGPTL4 (Human) IgG
Code No.: A00309-02-100
Size: 100 ug
Price: $220.00 USD
Host: Rabbit
Antigen:angptl4 Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: E, IHC, WB
Working Dilution: IHC 1: 500 (2 ug/ml)
Data Sheet: PDF
anti human angptl4 antibody for immunohistochemistry Anti ANGPTL4 (Human) IgG
Code No.: A00309-02-100
Size: 100 ug
Price: $220.00 USD
Host: Rabbit
Antigen:angptl4 Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: E, IHC, WB
Working Dilution: IHC 1: 500 (2 ug/ml)
Data Sheet: PDF
Anti ANGPTL4 (Human) IgG
Code No.: A00309-02-100
Size: 100 ug
Price: $220.00 USD
Host: Rabbit
Antigen:angptl4 Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: E, IHC, WB
Working Dilution: IHC 1: 500 (2 ug/ml)
Data Sheet: PDF
anti angptl4 monoclonal antibody Anti ANGPTL4 (Human) Monoclonal IgG1
Code No.: A00309-01-50
Size: 100 ug
Price: $260.00 USD
Host: Mice
Antigen: human angptl4 Rec.
Ab Type: Monoclonal IgG 1
Purification: Protein G
Applications: WB
Working Dilution:WB 1-5 ug/ml
Data Sheet: PDF
Anti ANGPTL4 (Rat) IgG
Code No.: A00309-06-100
Size: 100 ug
Price: $220.00 USD
Host: Rabbit
Antigen: rat angptl4 Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: E, IHC, WB
Working Dilution: IHC 5 ug/ml; WB 2-4 ug/ml
Data Sheet: PDF
   

 

Name
Code No.
Size
Price
Angiopoietin Like 4 (ANGPTL4) (Human) ELISA Kit
96 T
360.00
Angiopoietin Like 4 (Human) , Rec.
00309-01-10
10 ug
80.00
Angiopoietin Like 4 (Human) , Rec.
00309-01-50
50 ug
220.00
Angiopoietin Like 4 (Human) , Rec.
100 ug
360.00
Angiopoietin Like 4 (Human) , Rec. Biotinylated
00309-01-50B
50 ug
395.00
Angiopoietin Like 4 (Human) , Rec. Cy3 conjugated
00309-01-50C3
50 ug
460.00
Angiopoietin Like 4 (Human) , Rec. (human cell derived)
00309-04-10
10 ug
120.00
Angiopoietin Like 4 (Rat) , Rec.
100 ug
360.00
Angiopoietin Like 4 (Mouse) , Rec.
00309-03-50
50 ug
250.00
Angiopoietin Like 4 (Mouse) , Rec.
100 ug
360.00
Angiopoietin Like 4 (Mouse) , Rec. Biotinylated
00309-03-50B
50 ug
390.00
Angiopoietin Like 4 (Mouse) , Rec. FAM conjugated
00309-03-50FAM
50 ug
450.00
Angiopoietin Like 4 (Mouse) , Rec. FITC conjugated
00309-03-50FITC
50 ug
450.00
Angiopoietin Like 4 (Mouse) , Rec. Cy3 conjugated
00309-03-50C3
50 ug
550.00
Mouse Anti ANGPTL4 (Human) monoclonal IgG1
50 ug
260.00
Rabbit Anti ANGPTL4 (Human) IgG
100 ug
220.00
Rabbit Anti ANGPTL4 (Human) IgG, Biotinlyated
A00309-02-50B
100 ug
260.00
Rabbit anti ANGPTL4 (Mouse) IgG
100 ug
260.00
Rabbit Anti ANGPTL4 (Rat) IgG
100 ug
220.00