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CIDEC encodes a member of the cell death-inducing DNA fragmentation factor-like effector family. Zusätzlich bieten wir Ihnen CIDEC Proteine (8) und CIDEC Kits (1) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 89 products:
Human Polyclonal CIDEC Primary Antibody für ICC, IF - ABIN151889
Guillén, Navarro, Arnal, Noone, Arbonés-Mainar, Acín, Surra, Muniesa, Roche, Osada: Microarray analysis of hepatic gene expression identifies new genes involved in steatotic liver. in Physiological genomics 2009
Show all 4 Pubmed References
Human Polyclonal CIDEC Primary Antibody für WB - ABIN528484
Ito, Nagasawa, Omae, Ide, Akasaka, Murakami: Differential regulation of CIDEA and CIDEC expression by insulin via Akt1/2- and JNK2-dependent pathways in human adipocytes. in Journal of lipid research 2011
Human Monoclonal CIDEC Primary Antibody für ELISA, WB - ABIN528486
Christensen, Nellemann, Jørgensen, Pedersen, Jessen: Erythropoietin does not activate erythropoietin receptor signaling or lipolytic pathways in human subcutaneous white adipose tissue in vivo. in Lipids in health and disease 2016
Human Polyclonal CIDEC Primary Antibody für ICC, IF - ABIN4298770
Dabir, Kluge, McColl, Liu, Lam, Halmos, Wildey, Dowlati: PIAS3 activates the intrinsic apoptotic pathway in non-small cell lung cancer cells independent of p53 status. in International journal of cancer 2013
CIDEC may affect body measurement traits and meat quality traits in Qinchuan cattle, and could be used in marker-assisted selection.
This paper examined the tissue expression profile of CIDEC gene in cattle.
Two tissue-specific CIDEc isoforms had different roles in lipid deposition.
data suggested that Cidec could interact with and down-regulate AMPKalpha (zeige GRK4 Antikörper) through an ubiquitin-proteasome degradation pathway, which provided a possible mechanism of Cidec in promoting human adipocytes differentiation
Hepatic expression of FSP27/CIDEC is highly up-regulated in in patients with alcoholic steatohepatitis and this up-regulation contributes to alcohol-induced liver damage.
It is insinuated that VAT is associated with late phase obesity CIDEC decrease and insulin (zeige INS Antikörper) resistance, while pioglitazone enhances CIDEC through activation of PPAR-gamma (zeige PPARG Antikörper), increases its expression, and decreases lipolysis.
After bariatric surgery-induced weight loss, CIDEC/FSP27 gene/protein expression in SAT increased significantly. Findings suggest a positive functional interaction between CIDEC/FSP27 & mitochondrial biogenesis-related genes in human adipose tissue
Data indicate that fat-specific protein 27 (FSP27) increases the inhibitory effect of transcription factor Egr1 (zeige EGR1 Antikörper) on the adipose triglyceride lipase (ATGL (zeige PNPLA2 Antikörper)) promoter.
results demonstrate a crucial role for FSP27-ATGL (zeige PNPLA2 Antikörper) interactions in regulating lipolysis, triglyceride accumulation, and insulin (zeige INS Antikörper) signaling in human adipocytes
homo-dimeric structure of the CIDE-N domain of FSP27 will provide important information that will enable better understanding of the function of FSP27.
CIDE proteins expression correlate with tumor and survival characteristics in patients with renal cell carcinoma (zeige MOK Antikörper).
Fsp27/CIDEC is a CREB (zeige CREB1 Antikörper) target gene induced during early fasting in liver and regulated by FA oxidation rate.
Fatty acids prevent CIDEC deacetylation by promoting the dissociation of CIDEC from HDAC6 (zeige HDAC6 Antikörper), resultin in increased association of CIDEC with PCAF (zeige KAT2B Antikörper) on the endoplasmic reticulum.
We show that partial silencing Fsp27 in either model results in the robust decrease in visceral fat, improved insulin (zeige INS Antikörper) sensitivity and whole-body glycemic control, and tissue-specific changes in transcripts controlling lipid oxidation and synthesis
results suggest that FSP27beta negatively regulates CideA (zeige CIDEA Antikörper)-promoted enlargement of lipid droplet size in brown adipocytes.
Lipid droplet (LD) expansion depends on the FSP27 carboxy-terminal domain (amino acids 131-239). The negative charge of acidic residues D215, E218, E219 and E220 in the polar carboxy-terminal region (amino acids 202-239) is essential for LD enlargement.
Data (including data from studies in knockout mice) suggest Cideb (zeige CIDEB Antikörper) promotes lipid storage as droplets in hepatocytes under normal diet conditions; Cidea (zeige CIDEA Antikörper)/Cidec promote fusion of lipid droplets leading to liver steatosis in fasting (16h) and obese mice.
Cidea (zeige CIDEA Antikörper) is highly associated with adiposity and insulin (zeige INS Antikörper) resistance, whereas Cidec is related to insulin (zeige INS Antikörper) sensitivity
Hepatic expression of FSP27/CIDEC is highly up-regulated in mice following chronic-plus-binge ethanol feeding and this up-regulation contributes to alcohol-induced liver damage.
Insulin (zeige INS Antikörper) resistance and white adipose tissue inflammation are uncoupled in energetically challenged Fsp27-deficient mice.
CREBH (zeige CREB3L3 Antikörper)-Fsp27beta axis is important for regulating lipid droplet dynamics and triglyceride storage in the liver
Adipocyte-specific disruption of fat-specific protein 27 causes hepatosteatosis and insulin (zeige INS Antikörper) resistance in high-fat diet-fed mice.
CIDEC protects lipid droplets (LDs) by decreasing the specific surface area of LDs and is involved in the regulation of hepatic lipid deposition.
CIDEa (zeige CIDEA Antikörper) and CIDEc mRNA level in white adipose tissues and liver were significantly higher in obese pigs than in their lean counterparts
This gene encodes a member of the cell death-inducing DNA fragmentation factor-like effector family. Members of this family play important roles in apoptosis. The encoded protein promotes lipid droplet formation in adipocytes and may mediate adipocyte apoptosis. This gene is regulated by insulin and its expression is positively correlated with insulin sensitivity. Mutations in this gene may contribute to insulin resistant diabetes. A pseudogene of this gene is located on the short arm of chromosome 3. Alternatively spliced transcript variants that encode different isoforms have been observed for this gene.
cell death-inducing DFFA-like effector c
, cell death activator CIDE-3
, cell death-inducing DFFA-like effector protein C
, fat-specific protein FSP27 homolog
, Cell death activator CIDE-3
, fat specific protein 27
, fat specific gene 27
, fat-specific protein FSP27
, cell-death-inducing DNA-fragmentation-factor-like effector C