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Mouse Anti-CP Recombinant Antibody (CBFYC-2129) (V2LY-1206-LY887)


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Published Data
V2LY-1206-LY887-1
Mouse Anti-CP Recombinant Antibody (CBFYC-2129) (V2LY-1206-LY887) in WB
Immunodetection validation of vesicular proteins identified as potential biomarker candidates for brown adipose tissue (BAT) and white fat in the DIA-SWATH/MS analysis (sequential window acquisition of all theoretical fragment ions) in EVs secreted from 1 g of AT from obese and lean animals. Representative images are shown of: immunodetection. ...View More
Camino, T., Lago-Baameiro, N., Sueiro, A., Bravo, S. B., Couto, I., Santos, F. F., ... & Pardo, M. (2022). Brown adipose tissue sheds extracellular vesicles that carry potential biomarkers of metabolic and thermogenesis activity which are affected by high fat diet intervention. International Journal of Molecular Sciences, 23(18), 10826.
Distributed under Open Access license CC BY 4.0, without modification.
V2LY-1206-LY887-2
Mouse Anti-CP Recombinant Antibody (CBFYC-2129) (V2LY-1206-LY887) in WB
Confirmation of DIGE results by western-blot.
Detection and quantification of (A) carboxypeptidase-N (CPN), (B) serum paraoxonase /arylesterase 1 (PON1), and (C) ceruloplasmin (CP) in depleted human plasma samples previously analysed by DIGE. Protein band density was calculated by QuantityOne 4.4.0 (BioRad) software. Results are shown as arbitrary units (AU); (D) Transferred proteins to the nitrocellulose membrane were detected by Ponceau S stain as western-blot loading control. C1, C2 and C3: protein samples of patients from the control group; T1, T2 and T3: protein samples of patients from the tumor group. ...View More
Ferrin, G., Rodriguez-Peralvarez, M., Aguilar-Melero, P., Ranchal, I., Llamoza, C., Linares, C. I., ... & de la Mata, M. (2015). Plasma protein biomarkers of hepatocellular carcinoma in HCV-infected alcoholic patients with cirrhosis. PLoS One, 10(3), e0118527.
Distributed under Open Access license CC BY 4.0, without modification.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBFYC-2129
Antibody Isotype
IgG2b, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 121-180 of human ceruloplasmin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
0.1% gelatin
Preservative
0.09% sodium azide
Concentration
0.2 mg/ml
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Ceruloplasmin
Entrez Gene ID
Human1356
Mouse12870
Rat24268
UniProt ID
HumanP00450
MouseQ61147
RatP13635
Function
Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe2+ to Fe3+ without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu2+ 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 (By similarity).
Biological Process
Cellular iron ion homeostasis Source: Reactome
Cellular protein metabolic process Source: Reactome
Copper ion transport Source: UniProtKB-KW
Iron ion homeostasis Source: GO_Central
Iron ion transport Source: GO_Central
Post-translational protein modification Source: Reactome
Cellular Location
Secreted. Colocalizes with GCP1 in secretory intracellular compartments.
Involvement in disease
Aceruloplasminemia (ACERULOP):
An autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances.
More Infomation

Kang, N. L., Zhang, J. M., Lin, M. X., Chen, X. D., Huang, Z. X., Zhu, Y. Y., ... & Zeng, D. W. (2020). Serum ceruloplasmin can predict liver fibrosis in hepatitis B virus-infected patients. World Journal of Gastroenterology, 26(27), 3952.

Vlasova, I. I., Sokolov, A. V., Kostevich, V. A., Mikhalchik, E. V., & Vasilyev, V. B. (2019). Myeloperoxidase-induced oxidation of albumin and ceruloplasmin: role of tyrosines. Biochemistry (Moscow), 84(6), 652-662.

Wang, B., & Wang, X. P. (2019). Does ceruloplasmin defend against neurodegenerative diseases?. Current Neuropharmacology, 17(6), 539-549.

Tian, S., Jones, S. M., Jose, A., & Solomon, E. I. (2019). Chloride control of the mechanism of human serum ceruloplasmin (Cp) catalysis. Journal of the American Chemical Society, 141(27), 10736-10743.

Rydén, L. (2018). Ceruloplasmin. In Copper proteins and copper enzymes (pp. 37-100). CRC Press.

Zhao, Y. S., Zhang, L. H., Yu, P. P., Gou, Y. J., Zhao, J., You, L. H., ... & Chang, Y. Z. (2018). Ceruloplasmin, a potential therapeutic agent for Alzheimer's disease. Antioxidants & redox signaling, 28(14), 1323-1337.

Zheng, J., Chen, M., Liu, G., Xu, E., & Chen, H. (2018). Ablation of hephaestin and ceruloplasmin results in iron accumulation in adipocytes and type 2 diabetes. FEBS letters, 592(3), 394-401.

Golizeh, M., Lee, K., Ilchenko, S., Ösme, A., Bena, J., Sadygov, R. G., ... & Kasumov, T. (2017). Increased serotransferrin and ceruloplasmin turnover in diet-controlled patients with type 2 diabetes. Free Radical Biology and Medicine, 113, 461-469.

Squitti, R., Simonelli, I., Cassetta, E., Lupoi, D., Rongioletti, M., Ventriglia, M., & Siotto, M. (2017). Patients with increased non-ceruloplasmin copper appear a distinct sub-group of Alzheimer's disease: a neuroimaging study. Current Alzheimer Research, 14(12), 1318-1326.

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For research use only. Not intended for any clinical use.

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