Recombinant Human Ceruloplasmin (CP) Protein (His)

Name: Recombinant Human Ceruloplasmin (CP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07538P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ceruloplasmin (CP) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P00450
Target Symbol	CP
Synonyms	(Ferroxidase)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	ILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTLEMFPRTPGIWLLHCHVTDHIHAGM
Expression Range	807-1050aa
Protein Length	Partial
Mol. Weight	32.1 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense.
Subcellular Location	Secreted.
Protein Families	Multicopper oxidase family
Database References	HGNC: 2295 OMIM: 117700 KEGG: hsa:1356 STRING: 9606.ENSP00000264613 UniGene: PMID: 29127684 Maternal blood ceruloplasmin level was found to be lower in neural tube defect-affected pregnancies as compared to healthy controls. PMID: 28397206 Increased serum transferrin and ceruloplasmin turnover in diet-controlled patients with type 2 diabetes has been reported. PMID: 29079528 Strong correlations between the meconium concentrations of CP, LF and MPO indicate a possible role of these complementary proteins in maintaining homeostasis of the intrauterine environment of the fetus. CP, LF and MPO measured in meconium may serve as biomarkers for assessment of impairment of oxidative balance during intrauterine life with its potential impact on disease development in adulthood. PMID: 27903408 A woman in her 50s who initially presented with movement disorder was diagnosed with aceruloplasminemia, a rare autosomal recessive disorder resulting in accumulation of iron deposits in major organs. Genetic testing confirmed mutations in the ceruloplasmin gene (c.1864 + 1G>C). PMID: 27416276 Higher circulating ceruloplasmin levels were associated with increased atrial fibrillation risk. PMID: 28427851 for ATP7B mutations, the more severe impact on ATP7B protein was, the younger onset age and lower Cp level presented. The feasibility of presymptomatic DNA diagnosis and predicting clinical manifestation or severity of Wilson disease (WD) would be facilitated with identified mutations and genotype-phenotype correlation precisely revealed in the study. PMID: 27982432 Ceruloplasmin is supposed to be related with advanced T stage and perineural invasion, having a possibility as a candidate prognostic marker for bile duct cancer. PMID: 28423673 Mechanistically, ceruloplasmin could specifically interact with the hepatitis B virus middle surface protein. PMID: 28678687 The present study determined that ARE, CLP, CAT, and MPO levels are different between the pediatric patients with sepsis and healthy controls. ARE level can be a potent biomarker for sepsis in critical patients in intensive care units. PMID: 28167245 Ceruloplasmin was independently and negatively associated with liver fibrosis in chronic hepatitis b. PMID: 27920479 Coronary atherosclerosis is distinguished by serum C4 complement up-regulation and ceruloplasmin down-regulation. PMID: 28091899 Data show that the concentration of ceruloplasmin (ferroxidase; Cp) was significantly higher in Low hemoglobin (Hb) compared to High Hb subsample. PMID: 27235174 serum ceruloplasmin level was lower in the primary open-angle glaucoma group in comparison to the group with only cataract. PMID: 27109647 The determination of serum ceruloplasmin in adolescents might be a useful tool to identify patients with the highest risk of future cardiovascular disease. PMID: 27083758 The main result of this study is that ceruloplasmin specific activity is associated with a decreased risk of developing Alzheimer's disease PMID: 26836154 pathological cerebrospinal fluid's environment of Parkinson's disease patients promoted the same modifications in the exogenously added ceruloplasmin PMID: 26537957 Homozygosity for c.1948G>A is described in a Dutch family with aceruloplasminemia. PMID: 25661792 Cp-mediated neuroprotection occurs via the inhibition of seizure-associated oxidative damage. PMID: 25843655 PON-1 and ferroxidase activities in older patients with mild cognitive impairment, late onset Alzheimer's disease or vascular dementia PMID: 25490030 results of this study suggest that common genetic variants of CP are associated with PD and further investigation is needed to explore their functions in Parkinson disease. PMID: 25758665 we have through bioinformatic screening identified ceruloplasmin as a novel adipokine with increased expression in adipose tissue of obese subjects as well as in cells from obesity-associated cancers. PMID: 24676332 sLe(x)/CP ratio tended to be higher for the pancreatic adenocarcinoma PMID: 25595436 brain microvascular endothelial cell -secreted cytokine activity increases the gene expression of neighboring C6 glioma CP, which reciprocally acts on basolateral BMVEC ferroportin to enhance brain iron import PMID: 25311416 High ceruloplasmin levels are associated with preeclampsia. PMID: 25463281 Mercury metallation of the bacterial copper protein azurin is analogous to the one of human cerulopsmin and factor VIII in mercury poisoning. PMID: 25265377 A reduced serum FeOx activity, which can potentially lead to a rise in oxidative stress-induced biomolecular damage, seems to be a shared condition in inflammatory disorders of the central nervous system including MS. PMID: 25398823 This review describes the main role of ceruloplasmin in iron turnover is oxidizing Fe2+ into Fe3+, a process which is essential for iron binding to transferrin (the main iron-transporting protein), as well as to ferritin (the main iron-storage protein) PMID: 24988611 ceruloplasmin and hepcidin differentially regulate iron efflux from brain microvascular endothelial cells PMID: 24533165 The core-fucosylation ratio of ceruloplasmin increases significantly in alcohol-related hepatocellular carcinoma. PMID: 24799124 In CKD patients, increased serum ceruloplasmin, a regulator of nitric oxide activity, is associated with increased risk of long-term adverse cardiovascular events, even after multivariable model adjustment for traditional clinical/biologic risk factors. PMID: 24311705 Ceruloplasmin and gelsolin are closely interacted with the oncogene NF-kappab. PMID: 23925487 Increased urinary excretion of plasma proteins such as IgG, ceruloplasmin and transferrin, with different molecular radii of 55 A or less and different isoelectric points precede development of microalbuminuria in patients with NIDDM and hypertension. PMID: 24256706 The main result of this meta-analysis is that copper not bound to ceruloplasmin appears signi fi cantly increased in subjects with Alzheimer's disease when compared to healthy controls. PMID: 24072069 CP levels correlate negatively and indirectly with inflammation and fibrosis stages in male chronic hepatitis B patients. PMID: 24282481 both Cp NGR sites can deamidate during aging under oxidative conditions, likely as a consequence of oxidative-induced structural changes, thereby promoting a gain of function in integrin binding, signaling, and cell adhesion. PMID: 24366863 Findings indicate a causal role of ceruloplasmin in AF pathophysiology and suggest that ceruloplasmin might be a mediator in a specific inflammatory pathway that causally links inflammatory diseases and incidence of Atrial Fibrillation (AF). PMID: 24118451 A novel homozygous mutation of c.2185 delC in exon 12 was found in ceruloplasmin gene in a patient with aceruloplasminemia. PMID: 23812204 Eosinophil activation occurred in early and late responses after L-ASA NPT in upper airway mucosa of AERD patients, where ApoA1, alpha2M and CP as well as CysLT may be involved in eosinophilic inflammation. PMID: 23786280 The diffusion of an Fe(2+) ion from the inner opening of the human H-chain ferritin to a ferroxidase site located in the interior region of the protein coat is assisted by Thr135, His136 and Tyr137. PMID: 23344859 Ceruloplasmin was significantly elevated in patients with ischemic or nonischemic cardiomyopathy and had linear correlation with C-reactive protein and LVEF PMID: 23781119 Cp was associated with incident heart failure, mortality, and cardiovascular disease in the Atherosclerosis Risk in Communities population. PMID: 23861484 Data suggest that ceruloplasmin (CP) level in serum decreases according to severity of pediatric nonalcoholic fatty liver disease (NAFLD); thus, serum CP may serve as biomarker to discriminate children with severe NAFLD. PMID: 23154483 plasma ceruloplasmin is a potential plasma biomarker of aGvHD, and it also has prognostic value for risk-adapted prophylaxis. PMID: 23505556 Iron efflux from human brain microvasculature endothelial cells ferroportin requires the action of an exocytoplasmic ferroxidase which can be either endogenous hephaestin or extracellular ceruloplasmin. PMID: 23640881 study of effect of occupational exposure to lead among metallurgy workers in Poland on blood levels of transferrin (TRF), ceruloplasmin (CER) and haptoglobin (HPG): Data suggest that blood levels of copper and CER are raised with lead exposure. PMID: 22923205 ceruloplasmin should provide a protective shield against inadvertent oxidant production by myeloperoxidase during inflammation PMID: 23306200 Letter: report mutations in ceruloplasmin promoter in and possible role in iron hemostasis in patients with porphyria cutanea tarda. PMID: 23012398 study to determine if genetic variations identified in CP gene contribute to oesophageal cancer (OC) pathogenesis or susceptibility in Black Xhosa-speaking South African population; statistically significant associations found for 2 of the novel variants with OC in this study and could potentially contribute to disease susceptibility PMID: 21901748 change of the maintenance of three acute phase proteins: ceruloplasmin, alpha1-antitripsin and orosomucoid in an oral fluid and blood plasma at paradontitis and myocardial infarction PMID: 22708402

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.