SAB1400666
Monoclonal Anti-CIDEC antibody produced in mouse
clone 2E2, purified immunoglobulin, buffered aqueous solution
Sinónimos:
Anti-CIDE-3, Anti-FLJ20871, Anti-Fsp27
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Productos recomendados
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2E2, monoclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
indirect ELISA: suitable
western blot: 1-5 μg/mL
isotype
IgG1κ
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CIDEC(63924)
General description
CIDEC (cell death inducing DFFA (DNA fragmentation factor subunit α) like effector c) is mapped to human chromosome 3p25.3. The gene codes for FSP27 (fat-specific protein 27), also known as CIDEC. The encoded protein is localized to the lipid droplets surface. The gene is predominantly expressed in white adipose tissues and also expressed in liver and kidney.
Immunogen
CIDEC (NP_071377.2, 53 a.a. ~ 141 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Sequence
SVRKGIMAYSLEDLLLKVRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSEQGTRHPLSLSHKPAKKIDVA
Sequence
SVRKGIMAYSLEDLLLKVRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSEQGTRHPLSLSHKPAKKIDVA
Biochem/physiol Actions
CIDEC (cell death inducing DFFA (DNA fragmentation factor subunit α) like effector c) might be responsible for adipocytes differentiation. It is involved in the regulation of lipid droplet morphology and controls the lipid droplets size by inhibiting lipolysis. It is responsible for the triglycerides buildup in adipocytes. Upregulation of the gene is observed in obesity. Overexpression of the gene decreases the fatty acid oxidation (FAO) rate.
Cell death-inducing DFFA-like effector protein C (CIDEC) has a role in the differentiation of adipocytes. It associates with 5′ adenosine monophosphate-activated protein kinase (AMPK) α subunit 1 and acts as a negative regulator of the AMPK complex. CIDEC is also involved in lipid storage and it modulates the size of lipid droplets. The protein has been linked to obesity.
Physical form
Solution in phosphate buffered saline, pH 7.4
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Storage Class
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Bilal Haider Shamsi et al.
PloS one, 9(9), e106992-e106992 (2014-09-12)
Obesity is a metabolic disorder that can lead to high blood pressure, increased blood cholesterol and triglycerides, insulin resistance, and diabetes mellitus. The aim was to study the effects of pioglitazone mediated sensitization of peroxisome proliferator-activated receptor gamma (PPAR-γ) on
Ming Yu et al.
Molecular and cellular biochemistry, 378(1-2), 145-151 (2013-03-12)
Clear cell renal cell carcinoma (ccRCC) is the major and aggressive subtype of renal cell carcinoma. It is known to derive its histologic appearance from accumulation of abundant lipids and glycogens. The cell death-inducing DFF45-like effector (CIDE) family has been
Ming-Jiang Xu et al.
Gastroenterology, 149(4), 1030-1041 (2015-06-24)
Alcoholic steatohepatitis (ASH) is the progressive form of alcoholic liver disease and may lead to cirrhosis and hepatocellular carcinoma. We studied mouse models and human tissues to identify molecules associated with ASH progression and focused on the mouse fat-specific protein
Frederic Reinier et al.
Metabolism: clinical and experimental, 64(11), 1530-1540 (2015-09-10)
Lipodystrophies are a large heterogeneous group of genetic or acquired disorders characterized by generalized or partial fat loss, usually associated with metabolic complications such as diabetes mellitus, hypertriglyceridemia and hepatic steatosis. Many efforts have been made in the last years
Yuqiao Xu et al.
Biochimica et biophysica acta, 1850(12), 2552-2562 (2015-09-15)
We previously showed that Cidec was localized on the surface of lipid droplets and could promote the differentiation of human adipocytes, but the molecular mechanism was still unknown. In this study, we first sought to identify proteins that interact with
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