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Primary Antibodies  >  Infectious Disease Antibodies

Erpn/Ospe Antibody

Rabbit Polyclonal
NCI Collaboration
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Western blot showing detection of 0.1 µg recombinant proteins in Western blot.  Lane 1: Molecular weight markers.  Lane 2:  MBP-ErpN/OspE fusion protein (arrow; 59.5 kDa expected MW).  Lane 3:  fusion protein (MBP-tagged) plus cleaved fusion proteins (without MBP).  Lane 4:  MBP alone.  The lower bands are probably breakdown products.  The upper bands in lane 3 are fusion protein (top band), or breakdown products of the fusion protein (bands in middle of blot).  Protein was run on a 4-20% gel, then transferred to 0.45 µm nitrocellulose.  After blocking with 1% BSA-TTBS (p/n  MB-013, diluted to 1X) overnight at 4°C, primary antibody was used at 1:1000 at room temperature for 30 min.  HRP-conjugated Goat-Anti-Rabbit (p/n 611-103-122) secondary antibody was used at 1:40,000 in MB-070 blocking buffer and imaged on the VersaDoc™ MP 4000 imaging system (Bio-Rad).
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100 µg
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Erpn/Ospe Antibody Properties

Anti-ErpN/OspE (RABBIT) Antibody - 200-401-C10
Target Species
Borrelia burgdorferi
Known Cross Reactivity
Borrelia burgdorferi
ELISA : 1:5,000
Western Blot : 1:1,000
Other Dilution: User Optimized
Physical State
Shipping Condition
1.0 mg/mL by UV absorbance at 280 nm
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Reconstitution Volume
100 µL
Reconstitution Buffer
Restore with deionized water (or equivalent)
0.01% (w/v) Sodium Azide
erpN, BB_L39
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Erpn/Ospe Antibody Description

This product is antibody made against ErpN (OspE/F-Related Protein N), from the spirochete Borrelia burgdorferi, which is carried by Ixodes ticks. Erp proteins from Borrelia burgdorferi are postulated to be lipoproteins, based on their predicted amino acid sequences. The spirochete migrates from the tick midgut during feeding to its salivary glands and are thus transmitted to the mammal host. This transition may be facilitated by changes in expression of some B. burgdorferi genes. It is believed that expression of the various proteins associated with the spirochete may be regulated by the changes in tick life cycle, changes in conditions during tick feeding (such as temperature, pH, and nutrients) and/or in coordination with the course of infection of the mammal host. Several studies have demonstrated that infected humans and animals produce antibodies directed against Erp proteins within the first 2-4 weeks of infection, indicative of Erp synthesis during the initial stages of vertebrate infection. It is postulated that surface-exposed Erp proteins could facilitate interactions with host tissues during the establishment of vertebrate infection.
ErpN, ErpA, outer surface protein E, Borrelia burgdorferi OspE, ospE/F-Related Protein N
MBP-fusion protein corresponding to Borrelia burgdorferi ErpN/OspE protein.
Immunogen Type
Recombinant Protein
Storage Condition
Store vial at 4° C prior to restoration. For extended storage aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.
Application Note
Anti-ErpN/OspE antibody has been tested in Western Blot. Specific conditions for reactivity should be optimized by the end user. Expect a band at 17.1 kDa in size corresponding to ErpN/OspE by Western blotting in the appropriate cell lysate or extract.
This product was Protein-A purified and cross-adsorbed against MBP from monospecific antiserum by chromatography. It is directed against, and shows specific reactivity for, Borrelia burgdorferi OspE protein. Reactivity with ErpN/OspE protein from other sources has not been determined.
Disclaimer Note-General
This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
General Reference
Stevenson B., Tilly K, and Rosa PA (1996) A Family of Genes Located on Four Separate 32-Kilobase Circular Plasmids in Borrelia burgdorferi B31. J Bacteriology (178)12 3508-3516 Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. (1997) Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390:580-586
Specific Reference
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Secondary Antibodies;
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Conjugation Reference
Molecular Weight
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Conjugation Chemistry