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Surface Lipoprotein p27 Antibody Properties
Anti-Surface Lipoprotein p27 (RABBIT) Antibody - 200-401-C30S
Known Cross Reactivity
ELISA : >1:5,000
Western Blot : 1:1,000
Other Dilution: User Optimized
Liquid (sterile filtered)
1.0 mg/mL by UV absorbance at 280 nm
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
0.01% (w/v) Sodium Azide
UniProtKBNCBINCBI - NP_0457331.1UniProt - O50951Gene ID - 1194336
Surface Lipoprotein p27 Antibody Description
Surface Lipoprotein p27 of Borrelia burgdorferi is a surface-exposed lipoprotein that has been shown (by Western blot and Northern blot) to be expressed in the European B. burgdorferi strain B29, but not in the American strain B31. Cell envelope proteins of bacterial pathogens play important roles in the host-parasite interactions that occur during infection, including cell adherence, cell invasion, and immune cell activation or evasion. p27 is a basic protein of 248 amino acids with a typical prokaryotic leader sequence of 17 amino acid residues at the N-terminus of the proposed translation product. The p27 gene is located on a linear plasmid of a size of approximately 55 kb. Borrelia spirochetes are unique among diderm bacteria in their abundance of surface-displayed lipoproteins, some of which play important roles in the pathogenesis of Lyme disease and relapsing fever. There is evidence that Borrelia lipoproteins are specifically targeted to the bacterial surface, but that they can be retained in the periplasm by sequence-specific signals.
MBP-fusion protein corresponding to Borrelia burgdorferi Surface Lipoprotein p27 protein.
Store vial at -20 °C or below prior to opening. This vial contains a relatively low volume of reagent (25 µL). To minimize loss of volume dilute 1:10 by adding 225 µL of the buffer stated above directly to the vial. Recap, mix thoroughly and briefly centrifuge to collect the volume at the bottom of the vial. Use this intermediate dilution when calculating final dilutions as recommended below. Store the vial at -20°C or below after dilution. Avoid cycles of freezing and thawing.
Anti-Surface Lipoprotein p27 antibody has been tested in Western Blot. Specific conditions for reactivity should be optimized by the end user. Expect a band at ~30.9 kDa in size corresponding to p27 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 p27 protein. Reactivity with p27 protein from other sources has not been determined.
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 326, Gilbertsville, Pennsylvania, USA.
Reindl M, Redl B, Stöffler G. (1993) Isolation and analysis of a linear plasmid-located gene of Borrelia burgdorferi B29 encoding a 27 kDa surface lipoprotein (p27) and its overexpression in Escherichia coli. Mol Microbiol. 8(6):1115-24.
Schulze RJ, and Zückert WR (2006) Borrelia burgdorferi lipoproteins are secreted to the outer surface by default. Molecular Microbiology 59 (5), 1473 - 1484.
This product is offered by Biomol for research purposes only.
Not for diagnostic purposes or human use.
It may not be resold or used to manufacture commercial products without written approval of Biomol GmbH.