Purified anti-CD230 (Prion) Antibody (Previously Covance catalog# SIG-39620)

Pricing & Availability
3F4 (See other available formats)
Regulatory Status
Other Names
Major prion protein, p27-30, CD230 antigen, prion protein PrP, prion-related protein
Covance Catalog# SIG-39620
Signet Catalog# 9620-02
Signet Catalog# 9620-05
Signet Catalog# 9620-10
Mouse IgG2a, κ
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Product Citations
Human peripheral blood lymphocytes were stained with purified CD230 (clone 3F4, filled histogram) or purified mouse IgG2a, κ isotype control (open histogram), followed by anti-mouse IgG PE.
  • A_3F4_Purified_Prion_Antibody_2_010516
    Human peripheral blood lymphocytes were stained with purified CD230 (clone 3F4, filled histogram) or purified mouse IgG2a, κ isotype control (open histogram), followed by anti-mouse IgG PE.
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800310 50 µg 132€
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800301 200 µg 444€
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800302 500 µg 867€
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800303 1 mg 1424€
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Prions cause neurodegenerative disease by aggregating extracellularly within the central nervous system which disrupt the normal tissue structure. This disruption is characterized by "holes" in the tissue with resultant spongy architecture. Two conformational isoforms exist, the normal cellular isoform (PrPC) and the infectious, scrapie isoform (PrPSC). Other histological changes include astrogliosis and the absence of an inflammatory reaction. Neurodegenerative symptoms can include convulsions, dementia, ataxia (balance and coordination dysfunction), and behavioral or personality changes.

All known prion diseases are collectively called transmissible spongiform encephalopathies (TSEs). Prion (PrP) is highly conserved through mammals and comparison between primates ranges from 92.9-99.6% similarity in amino acid sequence. The human protein structure consists of a globular domain with three α-helices and a two-strand antiparallel β-sheet, an NH2-terminal tail, and a short COOH-terminal tail. A glycosylphosphatidylinositol (GPI) membrane anchor at the COOH-terminal tethers PrP to cell membranes. This anchor is integral to the transmission of conformational change; secreted PrP lacking the anchor component is unaffected by the infectious isoform. PrPSC accumulates in compact, protease-resistant aggregates within neural tissue and has a different secondary and tertiary structure from PrPC, but an identical primary sequence.

The primary sequence of PrP is 253 amino acids long before posttranslational modification. Signal sequences in the amino- and carboxy- terminal ends are removed posttranslationally, resulting in a mature length of 208. For human and Syrian hamster PrP, two glycosylated sites exist on helices 2 and 3 at Asn181 and Asn197. Murine PrP has glycosylation sites as Asn180 and Asn196. A disulfide bond exists between Cys179 of the second helix and Cys214 of the third helix (human PrPC numbering).

The precise function of PrP is not yet known, but it is possibly involved in the transport of ionic copper to cells from the surrounding environment. Researchers have also proposed roles for PrP in cell signaling or in the formation of synapses.

Spatial learning, a predominantly hippocampal-function, is decreased in PrP null mice and can be recovered with the reinstatement of PrP in neurons; indicating that loss of PrP function is the cause. PrP is present in both pre- and post-synaptic neuron cells, and the greatest concentration is in the pre-synaptic cells. Some research indicates PrP involvement in neuronal development, differentiation, and neurite outgrowth. The PrP-activated signal transduction pathway is associated with axon and dendritic outgrowth with a series of kinases.

Though most attention is focused on PrP’s presence in the nervous system, it is also abundant in immune system tissue. PrP immune cells include haematopoietic stem cells, mature lymphoid and myeloid compartments, and certain lymphocytes; also, it has been detected in natural killer cells, platelets, and monocytes. T cell activation is accompanied by a strong up-regulation of PrP, though it is not requisite. The lack of immuno-response to transmissible spongiform encephalopathies (TSE), neurodegenerative diseases caused by prions, could stem from the tolerance for PrPSc.

Product Details
Technical Data Sheet (pdf)

Product Details

Verified Reactivity
Antibody Type
Host Species
Phosphate-buffered solution.
The antibody was purified by affinity chromatography.
2 mg/ml
Storage & Handling
Do not store antibody diluted below 50 µg/mL in the absence of protein (i.e. add 2% bovine serum albumin). The antibody solution should be stored undiluted between 2°C and 8°C. Please note the storage condition for this antibody has been changed from -20°C to between 2°C and 8°C. You can also check your vial or your CoA to find the most accurate storage condition for this antibody.

FC - Quality tested
ELISA, WB, IHC-F, IP - Reported in the literature, not verified in house

Recommended Usage

Each lot of this antibody is quality control tested by immunofluorescent staining with flow cytometric analysis. For flow cytometric staining, the suggested use of this reagent is ≤0.25 µg per million cells in 100 µl volume. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

Additional reported applications (for the relevant formats) include: immunoblotting, immunohistochemistry on frozen tissue sections (IHC-F), immunoprecipitation (IP) and ELISA. 

3F4 is reactive to amino acid residues 109-112 of prion protein (PrP) from humans, hamsters, and felines. It recognizes both protease sensitive and protease resistant forms of PrP (after denaturing).

Application References
  1. Kondoh G, et al. 2005. Nat. Med. 11(2):160-6. (IHC-F)
  2. Gilch S, et al. 2004. Traffic. 5(4):300-13. (WB, IHC-F, ELISA) PubMed
  3. Nishina K, et al. 2004. Biochemistry 43:2613-21. (IP)
  4. Shiga Y, et al. 2004. Neurology 63(3):443-9. (WB, IHC-F, IP, ELISA)
  5. Zou WQ, et al. 2004. Proc. Natl. Acad. Sci. USA 101(5):1380-5.
  6. Kitamoto T, et al. 1987. Lab Invest. 57(2):230-6.
  7. Kascsak RJ, et al. 1987. J. Virol. 61(12):3688-93.
Product Citations
  1. Takahashi RH, et al. 2021. Brain Pathol. 31:e12941. PubMed
  2. Gilch S, et al. 2004. Traffic. 5:300-313. PubMed
AB_2715841 (BioLegend Cat. No. 800310)
AB_2564630 (BioLegend Cat. No. 800301)
AB_2564631 (BioLegend Cat. No. 800302)
AB_2564629 (BioLegend Cat. No. 800303)

Antigen Details

Biology Area
Cell Biology, Immunology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
Prion (CD230)
Antigen References

1. Asante EA, et al. 2015. Nature 522:478.
2. Mead S, et al. 2013. N. Engl. J. Med. 369:1904.
3. Chakrabarti O, Hegde RS. 2009. Cell 137:1136.
4. Wadsworth JD, et al. 2004. Science 306:1793.

Gene ID
5621 View all products for this Gene ID
View information about CD230 on UniProt.org

Related FAQs

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Go To Top Version: 6    Revision Date: 10/10/2018

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This data display is provided for general comparisons between formats.
Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors.
If you need assistance with selecting the best format contact our expert technical support team.

  • Purified anti-CD230 (Prion)

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  • FITC anti-human CD230 (Prion)

  • APC anti-human CD230 (Prion)

  • PE anti-human CD230 (Prion)


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