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Validated All-in-One™ qPCR Primer for CP(NM_000096.3) Search again
Product ID:
HQP002820
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AB073614, CP-2
Gene Description:
ceruloplasmin
Target Gene Accession:
NM_000096.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
The protein encoded by this gene is a metalloprotein that binds most of the copper in plasma and is involved in the peroxidation of Fe(II)transferrin to Fe(III) transferrin. Mutations in this gene cause aceruloplasminemia, which results in iron accumulation and tissue damage, and is associated with diabetes and neurologic abnormalities. [provided by RefSeq].
Gene References into function
- CERULOPLASMIN haS a role in iron uptake rather than release in BT325 cells.
- difference in the molecular structure between human and bovine ceruloplasmin using SDS-PAGE and MALDI-TOF mass spectrometry
- gene coding and flanking regions were sequenced and examined for mutations that might modulate the iron burden of individuals harboring the common mutant hemochromatosis HFE genotype or cause hemochromatosis independent of mutations in the HFE gene
- Studies of the ceruloplasmin-lactoferrin complex
- results show that insulin functions as a bidirectional, condition-dependent regulator of hepatic cell Cp expression; the unique regulation of Cp may reflect its dual roles in inflammation and iron homeostasis
- Carnosine, homocarnosine and anserine significantly inhibited the aggregation of CP induced by peroxyl radicals.
- Serum levels of soluble intercellular adhesion molecule-1 (sICAM-1), ceruloplasmin (Cp), and transferrin (Tf) in rheumatoid arthritis. Serum Tf levels were significantly diminished and serum levels of sICAM-1 and Cp were significantly increased.
- the three-copper cluster at the N-terminal-C-terminal interface plays a crucial role in the structural stability of human ceruloplasmin
- elucidation of mechanisms of copper incorporation
- Determination of specific antioxidants like ceruloplasmin in serum may be of value in the early diagnosis of prostate and colon cancer.
- data show that ceruloplasmin stimulates iron release from macrophages under hypoxic conditions by a ferroxidase-dependent mechanism
- Haptoglobin polymorphism was correlated with ceruloplasmin ferroxidase activity in a sample population of unrelated black Jordanians and activity is both haptoglobin type and concentration dependent.
- Urinary levels are increaed in normoalbuminuric type 2 diabetic patients.
- 5 new missense (I63T, P477L, T551I, R793H, T841R) & 3 new silent variations (g:9230/C->A, g:42221/C->T, g:4400/T->C) were found. Cp colocalized with Fe in Lewy bodies, suggesting a role in pathogenesis of Parkinson disease.
- REVIEW: mechanism for the involvement of ceruloplasmin in cardiovascular disease
- hypoxia-inducible factor (HIF)-1 has a role in ceruloplasmin regulation
- Cp polypeptides with molecular weight of nearly 30 kDa were found in mitochondria of HuTu 80 cells
- altered activity of ceruloplasmin may present a vulnerability factor for iron induced oxidative stress in Parkinson's disease
- Increased levels in urine predicts development of microalbuminuria in type 2 diabetes.
- results showed that exposure of CP to methylglyoxal led to protein aggregation and that aggregation of CP induced the inactivation of feroxidase and the release of copper ions
- Results describe the biochemical features of wild-type and mutant GPI-anchored ceruloplasmin.
- A biochemical analysis of the patients' serum and a biogenesis study of G969S mutant ceruloplasmin using mammalian cell culture system resulted in the synthesis and secretion of only apoceruloplasmin without any ferroxidase activity.
- In a Chinese woman who had diabetes mellitus, undetectable ceruloplasmin, hand tremor, neck dystonia, and cognitive disturbances, genetic analyses revealed a novel homozygous mutation (848G > C or W283S) in exon 5 in the ceruloplasmin gene.
- ceruloplasmin gene is regulated by activator protein-1 site in the gene by redox active copper.
- CP levels wefre determined in children with Henoch-Schonlein purpura.
- describe a study of the conformation of the human lactoferrin/ceruloplasmin complex in solution using small angle X-ray scattering
- The truncated mutant containing Cys-881 was able to pass through the ER and was secreted, while the truncated mutant protein without Cys-881 appeared to accumulate in the ER thus leading to ER stress and eventually resulting in cell death.
- In vitro equilibrium unfolding of CP involves intermediates and the copper ions are removed in stages.
- With regard to septic liver dysfunction, signs of cholestasis were mostly reflected in greater increases in Cp
- In contrast, apo-CP unfolds rapidly: the denatured state is reached in <2 days at 37 degrees C.
- The involvement of lymphocyte-derived CP on host defense processes via its anti/prooxidant properties is proposed, giving further support for a close functional interaction between the immune system and the Fe metabolism.
- stable complex between these Cp and Hp and Tf does not occur under the experimental conditions used
- In the cerebrospinal fluid of Alzheimer's disease patients the decrease of active CP, associated with the increase in the pool of copper not sequestered by this protein, may play a role in the neurodegenerative process
- Measurement of Cp separated by the present method could be useful for the diagnosis of ITP in the presence of thrombocytopenia and a non- or low-inflammatory state
- We report two siblings with markedly different phenotypes carrying a novel mutation: a homozygous deletion of two nucleotides (1257-1258 TT del) causing the premature stop of the Cp protein translation (Y401X).
- Multiple motor system dysfunction associated with a heterozygous ceruloplasmin gene mutation.
- Results describe the activity of ferroxidase, SOD1, and cofactors in CSF of patients with Parkinson's disease, Alzheimer's disease, Huntington's disease, or amyotrophic lateral sclerosis.
- Investigated of brain iron levels in two asymptomatic young adult carriers with heterozygous mutations of Cp gene by using T2*-weighted MR images.
- Ceruloplasmin is a better predictor of the long-term prognosis compared with fibrinogen, CRP, and IL-6 in patients with severe unstable angina.
- there is an increase in ceruloplasmin levels in placental tissue in preeclampsia compared to preterm and normal controls
- Antagonism of hyaluronan interactions with short-fragment hyaluronan oligomers decreased ceruloplasmin expression in parental and stem-like glioma cells in vivo and in cell culture, implying that hyaluronan regulates ceruloplasmin expression
- ROS affects RNA-protein complex formation to promote Cp mRNA decay.
- The contact between CP and MPO probably entails conformational changes close to the p-phenylenediamine binding site in CP, which explains the observed activation by MPO of the substrate's oxidation
- Ceruloplasmin fragmentation is implicated in 'free' copper deregulation of Alzheimer's disease.