Recombinant Mouse Ceruloplasmin (Cp), partial

Code CSB-YP736806MO
MSDS
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP736806MO
MSDS
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP736806MO-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP736806MO
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP736806MO
MSDS
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
Cp
Uniprot No.
Alternative Names
Cp; Ceruloplasmin; EC 1.16.3.1; Ferroxidase
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

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.
Gene References into Functions
  1. We thus used hephaestin (Heph) and ceruloplasmin (Cp) single-knockout mice and Heph/Cp double-knockout mice to investigate the roles of multicopper ferroxidases(MCF) in pancreatic iron homeostasis. We found that both HEPH and CP were expressed in the mouse pancreas, and that ablation of either MCF had limited effect on the pancreatic iron levels. PMID: 29883959
  2. Hephaestin and ceruloplasmin have roles in facilitating iron metabolism in the mouse kidney PMID: 27991585
  3. In D-galactosamine-sensitized mice CP+Cu(II) increased the LPS-induced lethality from 54 to 100%, while administration of antibodies against MIF prevented the lethal effect. The enhancement by CP+Cu(II) of the pro-inflammatory signal of MIF is discussed PMID: 26091949
  4. mice with mutation of Cp and Heph, iron accumulates in glia, while neurons have low iron levels. Both neurons and glia degenerate and mice become ataxic unless given an iron chelator. PMID: 26303407
  5. Data (including data from studies in knockout mice) suggest that ceruloplasmin and hephaestin play distinct roles in regulation of gene expression in various regions of the brain and are involved in iron homeostasis. PMID: 25788583
  6. an increase in Cp expression could contribute to tissue damage in early experimental autoimmune encephalomyelitis PMID: 24615902
  7. Evidence supports a regulatory role of both proteins (Ceruloplasmin (CP) and beta-amyloid protein precursor (APP)) in defence against iron-induced oxidative damage after TBI, which presents as a tractable therapeutic target. PMID: 24509156
  8. Genetic interactions between Cp, Mon1a, and the Slc40a1 locus are involved in iron metabolism. PMID: 24121729
  9. ceruloplasmin should provide a protective shield against inadvertent oxidant production by myeloperoxidase during inflammation PMID: 23306200
  10. The mouse ceruloplasmin gene has been mapped to chromosome 3. PMID: 178338
  11. Data found an increase in ceruloplasmin levels in the plasma of Npc1 -/- mice compared to Npc1 +/+ mice, and this increase was statistically significant (*p < 0.05). PMID: 22526561
  12. Cp and Heph are necessary for iron export from the retina but are not essential for iron import into the retina. PMID: 22342521
  13. levels of 5HT and norepinephrine and the expression of BDNF and its receptor trkB, are significantly reduced in the hippocampus of ceruloplasmin knockout mice PMID: 22035068
  14. Ceruloplasmin deficiency reduces levels of iron and BDNF in the cortex and striatum of young mice and increases their vulnerability to stroke. PMID: 21949858
  15. Ceruloplasmin stimulation of reelin cleavage is in line with a possible role of ceruloplasmin in nervous system development. PMID: 20188154
  16. Reduction in Cp is a sensitive biomarker for copper deficiency. PMID: 20170749
  17. mainly acts to release iron from cells in the liver PMID: 12393173
  18. Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. PMID: 12743117
  19. Cp has a pro-aggregative action on newly differentiated neurons in vitro specific for Cp in a concentration-dependent and saturable fashion. PMID: 12946701
  20. The copper-containing yeast protein Fet3p can restore iron homeostasis in phlebotomized mice with a deletion of the ceruloplasmin gene. PMID: 14739215
  21. Ceruloplasmin ane hephaestin are critical for CNS iron homeostasis and that loss of Cp and Heph in the mouse leads to age-dependent retinal neurodegeneration. PMID: 15365174
  22. Iron accumulation is reflected in increased ferritin expression in ceruloplasmin deficient mice and is accompanied by cell loss. PMID: 16988052
  23. the concentrations of ceruloplasmin and lactoferrin in milk were increased fivefold and more than 38-fold, respectively, within 48 h after weaning PMID: 16989572
  24. Transcripts of ceruloplasmin, involved in iron efflux, were overexpressed in periportal areas and the result was confirmed by in situ hybridization study. PMID: 18222182
  25. ROS affects RNA-protein complex formation to promote Cp mRNA decay. PMID: 19019832
  26. Datan confirmed that mouse ceruloplasmin had ferroxidase activity but revealed an additional ferroxidase in ceruloplasmin knockout mouse plasma. PMID: 19076073
  27. Microglial and endothelial induction of Cp is a neuroprotective mechanism during inflammation because Cp-deficient mice exhibited increased iron accumulation and demyelination when exposed to LPS and neurovascular reactivity to pneumococcal meningitis PMID: 17375196
  28. To elucidate the role of ceruloplasmin in copper metabolism, the kinetics of copper absorption, transport, distribution, and excretion were examined utilizing (64)Cu in wild-type and aceruloplasminemic mice PMID: 11461924

Show More

Hide All

Subcellular Location
Secreted.
Protein Families
Multicopper oxidase family
Tissue Specificity
Expressed in many tissues, including liver, eye and brain.
Database Links
CUSABIO guaranteed quality
icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2025 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1