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Rabbit Anti-CIDEC Antibody (CSB-PA842636ESR1HU)
Supplier: CUSABIO BIOTECH CO.
Cell death-inducing DFFA-like effector protein C Antibody,Fat-specific protein FSP27 homolog Antibody,CIDEC Antibody,FSP27 AntibodyMore alternative names for the antibody
Cell death activator antibody|Cell death activator CIDE-3 antibody|Cell death inducing DFFA like effector C antibody|Cell death inducing DFFA like effector protein C antibody|Cell death-inducing DFFA-like effector protein C antibody|CIDE 3 antibody|CIDE3 antibody|CIDEC antibody|CIDEC_HUMAN antibody|Fat specific protein 27 antibody|Fat-specific protein FSP27 homolog antibody|FLJ20871 antibody|FPLD5 antibody|FSP27 antibody
Anti-CIDE C antibody (ab77115)
Anti-CIDE C antibody (ab77115)
Recommended applications: ELISA, IHC
Recommended dilution: Recommended dilution:IHC:1:20-1:200
Recommended protocols: check protocols
|Catalogue No.|| |
Recombinant human Cell death activator CIDE-3 protein (1-238AA)
|Recommended dilution|| |
|Molecular weight|| |
Antigen Affinity Purified
Shipped at 4 Celcius Degree. Upon delivery aliquot and store at -20 Celcius Degree or -80 Celcius Degree. Avoid repeated freeze.
|Database links|| |
Entrez Gene:63924( Human), Entrez Gene:14311( Mouse), Entrez Gene:100127161( Pig), Omim:612120( Human), SwissProt:Q96AQ7( Human), SwissProt:P56198( Mouse), Unigene:567562( Human), Unigene:635072( Human), Unigene:10026( Mouse)
|Protein function|| |
Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression. .
|Protein tissue specificity|| |
Expressed mainly in adipose tissue, small intestine, heart, colon and stomach and, at lower levels, in brain, kidney and liver. .
|Involvement in disease|| |
Note=In omental adipose tissue of obese patients matched for BMI, expression levels tend to correlate with insulin sensitivity. Expression is increased 2-3 fold in the group of patients with high insulin sensitivity, compared to the insulin-resistant group. This observation is consistent with the idea that triglyceride storage in adipocytes plays an important role in sequestering triglycerides and fatty acids away from the circulation and peripheral tissues, thus enhancing insulin sensitivity in liver and muscle. This effect is not significant in subcutaneous adipose tissue (PubMed:18509062). In subcutaneous adipose tissue of diabetic patients, tends to negatively correlate with body mass index and total fat mass, independently of insulin sensitivity (PubMed:18334488). .; Lipodystrophy, familial partial, 5 (FPLD5) [MIM:615238]: A form of lipodystrophy characterized by loss of subcutaneous adipose tissue affecting limb, femorogluteal and subcutaneous abdominal fat, preservation of visceral, neck and axilliary fat, hepatomegaly, hepatic steatosis and insulin-resistant diabetes. . Note=The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
The CIDE-N domain is involved in homodimerization which is crucial for its function in promoting lipid exchange and transfer.
|Protein post-translational modifications|| |
Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life. Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation (By similarity). .
|Protein cellular localization|| |
Nucleus . Endoplasmic reticulum. Lipid droplet. Note=Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites.
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|Product type|| |
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