CD230 / PrP antibody

Principal name

CD230 / PrP antibody

Alternative names for CD230 / PrP antibody

Major prion protein, PrP27-30, PrP33-35C, ASCR, PRNP, PRIP

SwissProt ID

O18754 (Felca), O46501 (Canfa), P04156 (Human), P04925 (Mouse), P10279 (Bovin), P13852 (Rat), P23907 (Sheep)

Gene ID

493887 (PRNP), 5621, 281427, 19122 (Prnp), 24686

Available reactivities

Hu (Human), Ms (Mouse), Rt (Rat), Sh (Sheep), Bov (Bovine), Hst (Hamster), Deer, Por (Porcine), Can (Canine), Gt (Goat), Fe (Feline)

Available hosts

Mouse, Goat, Rabbit, Chicken

Available applications

Western blot / Immunoblot (WB), Enzyme Immunoassay (E), Paraffin Sections (P), Frozen Sections (C), Immunoprecipitation (IP), Immunocytochemistry/Immunofluorescence (ICC/IF)

Background of CD230 / PrP antibody

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 alpha;-helices and a two-strand antiparallel beta;-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 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 rsquo;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 lymphoc

General readings

1. Bounhar, Y., Zhang, Y., Goodyer, C. G., LeBlanc, A.Prion protein protects human neurons against
Bax-mediated apoptosis.J. Biol. Chem. 276: 39145-39149, 2001.
2. Brown, P., Galvez, S., Goldfarb, L. G., Nieto, A., Cartier, L., Gibbs, C. J., Jr., Gajdusek, D. C.Familial
Creutzfeldt-Jakob disease in Chile is associated with the codon 200 mutation of the PRNP amyloid
precursor gene on chromosome 20.J. Neurol. Sci. 112: 65-67, 1992.
3. Puckett, C., Concannon, P., Casey, C., Hood, L.Genomic structure of the human prion protein
gene.Am. J. Hum. Genet. 49: 320-329, 1991.

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Primary Antibodies

Catalog No. Host Iso. Clone Pres. React. Applications  

CD230 / PrP antibody

Rat brain lysate was resolved by electrophoresis, transferred to PVDF and probed with anti-Prion Protein, clone 2G11 (1 µg/mL). Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and a chemiluminescence detection system. Arrow indicates Prion Protein (~27 kDa) Mouse IgG2a 2G11 Purified Hu, Ms, Rt, Sh E, P, WB
0.25 mg / €430.00
  Acris Antibodies GmbH

CD230 / PrP antibody

Western blotting analysis of Creutzfeld-Jakob disease (CJD) negative (lane 1, 2) and CJD positive (lane 3, 4) human brain material using anti-PrP antibody (clone EM-20). CJD positive patient has proteinase K resistent prion protein.
Lane 1, 4: Samples with proteinase K treatment
Lane 2, 3: Samples without proteinase K treatment Mouse IgG2a EM-20 Aff - Purified Hu P, WB
0.1 mg / €310.00
  Acris Antibodies GmbH

CD230 / PrP (N-term) antibody

Western blot analysis of Prion protein using Prion antibody (DB 033) was performed by Drs. Valeriy Ostapchenko and Marco Prado, Robarts Research Institute, the University of Western Ontario, London, Ontario, Canada. Lanes A-C represent extracts (30 μg of total protein per lane) of PrP-KO CF-10 cells (A), Mouse hippocampus (B) and HEK293 cells, transfected with Mouse prion protein bearing 3F4 epitope (C), Lane D corresponds to 30 ng recombinant MoPrP. Rabbit T16-R Aff - Purified Bov, Hu, Ms, Rt C, E, IP, P, WB
0.1 ml / €510.00
  DB Biotech, spol. s r.o.

Sample sizes available

CD230 / PrP (N-term) antibody

Western blot analysis of Prion protein using Prion antibody (DB 033) was performed by Drs. Valeriy Ostapchenko and Marco Prado, Robarts Research Institute, the University of Western Ontario, London, Ontario, Canada. Lanes A-C represent extracts (30 μg of total protein per lane) of PrP-KO CF-10 cells (A), Mouse hippocampus (B) and HEK293 cells, transfected with Mouse prion protein bearing 3F4 epitope (C), Lane D corresponds to 30 ng recombinant MoPrP. Rabbit T16-R Aff - Purified Bov, Hu, Ms, Rt C, E, IP, P, WB
50 µl / €350.00
  DB Biotech, spol. s r.o.

Sample sizes available

CD230 / PrP antibody

Western blot analysis of Prion protein using Prion antibody (DB 033) was performed by Drs. Valeriy Ostapchenko and Marco Prado, Robarts Research Institute, the University of Western Ontario, London, Ontario, Canada. Lanes A-C represent extracts (30 μg of total protein per lane) of PrP-KO CF-10 cells (A), Mouse hippocampus (B) and HEK293 cells, transfected with Mouse prion protein bearing 3F4 epitope (C), Lane D corresponds to 30 ng recombinant MoPrP. Rabbit V21-V Aff - Purified Bov, Hu, Ms, Rt C, E, IP, P, WB
0.1 ml / €530.00
  DB Biotech, spol. s r.o.

Sample sizes available

CD230 / PrP antibody

Western blot analysis of Prion protein using Prion antibody (DB 033) was performed by Drs. Valeriy Ostapchenko and Marco Prado, Robarts Research Institute, the University of Western Ontario, London, Ontario, Canada. Lanes A-C represent extracts (30 μg of total protein per lane) of PrP-KO CF-10 cells (A), Mouse hippocampus (B) and HEK293 cells, transfected with Mouse prion protein bearing 3F4 epitope (C), Lane D corresponds to 30 ng recombinant MoPrP. Rabbit V21-V Aff - Purified Bov, Hu, Ms, Rt C, E, IP, P, WB
50 µl / €350.00
  DB Biotech, spol. s r.o.

Sample sizes available

CD230 / PrP (C-term) antibody

Western blot analysis of Prion protein using Prion antibody (DB 081) was performed by Drs. Valeriy Ostapchenko and Marco Prado, Robarts Research Institute, the University of Western Ontario, London, Ontario, Canada. Lanes A-C represent extracts (30 μg of total protein per lane) of PrP-KO CF-10 cells (A), Mouse hippocampus (B) and HEK293 cells, transfected with Mouse prion protein bearing 3F4 epitope (C), Lane D corresponds to 30 ng recombinant MoPrP. Rabbit C16-S Aff - Purified Bov, Hu, Ms C, E, IP, P, WB
0.1 ml / €530.00
  DB Biotech, spol. s r.o.

Sample sizes available

CD230 / PrP (C-term) antibody

Western blot analysis of Prion protein using Prion antibody (DB 081) was performed by Drs. Valeriy Ostapchenko and Marco Prado, Robarts Research Institute, the University of Western Ontario, London, Ontario, Canada. Lanes A-C represent extracts (30 μg of total protein per lane) of PrP-KO CF-10 cells (A), Mouse hippocampus (B) and HEK293 cells, transfected with Mouse prion protein bearing 3F4 epitope (C), Lane D corresponds to 30 ng recombinant MoPrP. Rabbit C16-S Aff - Purified Bov, Hu, Ms C, E, IP, P, WB
50 µl / €350.00
  DB Biotech, spol. s r.o.

Sample sizes available

CD230 / PrP (143-153) antibody

  Goat Polyclonal Antibody against Prion Protein (143-153)  
TA302683 (0.3µg/ml) staining of Human Brain lysate (35µg protein in RIPA buffer).  Primary incubation was 1 hour.  Detected by chemiluminescence. Goat Aff - Purified Bov, Hu, Por E, WB
0.1 mg / €325.00
  OriGene Technologies, Inc.

CD230 / PrP antibody

  Rabbit anti-PRNP Polyclonal Antibody  
Western blot analysis of extracts of various cell lines, using PRNP antibody. Rabbit IgG Purified Hu, Ms, Rt
0.1 mg / €325.00
  OriGene Technologies, Inc.

CD230 / PrP antibody

  Rabbit Polyclonal Prion protein Antibody  
Western Blot: Prion protein Antibody [TA336429] - analysis of BSE in (A) recombinant fusion protein containing amino acids 142-148 and (B) fusion partner without these amino acids, using this antibody. 5 ug/ml. Rabbit Purified Bov, Sh WB
0.1 mg / €325.00
  OriGene Technologies, Inc.

CD230 / PrP antibody

  Rabbit Polyclonal Prion protein Antibody  
Western Blot: Prion protein Antibody [TA336430] - Analysis of BSE in (A) recombinant fusion protein containing amino acids 162-170 and (B) fusion partner without these amino acids, using this antibody at 5 ug/ml. Rabbit Purified Bov, Sh WB
0.1 mg / €325.00
  OriGene Technologies, Inc.

CD230 / PrP antibody

  Rabbit Polyclonal Prion protein Antibody  
Western Blot: Prion protein Antibody [TA336431] - analysis of BSE in (A) recombinant fusion protein containing amino acids 217-229 and (B) fusion partner without these amino acids, using this antibody. 5 ug/ml. Rabbit Purified Bov, Sh WB
0.1 mg / €325.00
  OriGene Technologies, Inc.

CD230 / PrP antibody

  Rabbit Polyclonal Anti-PRNP Antibody  
Host: Rabbit; Target Name: Prnp; Sample Tissue: Mouse Kidney lysates; Antibody Dilution: 1.0 ug/ml Rabbit IgG Purified Bov, Can, Gt, Hu, Rt, Sh WB
50 µg / €325.00
  OriGene Technologies, Inc.

CD230 / PrP antibody

  Rabbit Polyclonal Prion protein Antibody  
ELISA: Prion protein Antibody Rabbit IgG Purified Hu E
0.1 mg / €325.00
  OriGene Technologies, Inc.

CD230 / PrP (93-109) antibody

CD230 / PrP Mouse IgG2a 6D11 Purified Bov, Hst, Hu, Ms, Sh C, E, WB
0.1 ml / €1,100.00
  Acris Antibodies GmbH

CD230 / PrP antibody

CD230 / PrP Mouse IgG1 5121 Purified Bov, Sh E, P, WB
0.1 mg / €440.00
  Acris Antibodies GmbH

CD230 / PrP antibody

CD230 / PrP Goat IgG Serum Bov, Hst, Hu, Sh E, P, WB
0.1 ml / €330.00
  Acris Antibodies GmbH

CD230 / PrP antibody

CD230 / PrP Goat IgG Serum Bov, Hst, Hu, Sh P
10 µl / €200.00
  Acris Antibodies GmbH

CD230 / PrP antibody

Cultured fibroblasts cells transiently transfected with a plasmid containing the Prion Protein cDNA Chicken Ig Purified Hu, Ms, Rt ICC/IF, WB
0.2 ml / €340.00
  Acris Antibodies GmbH

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