product summary
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company name :
Rockland Immunochemicals
product type :
antibody
product name :
OspB Antibody
catalog :
200-401-C15
quantity :
100 µg
clonality :
polyclonal
host :
domestic rabbit
conjugate :
nonconjugated
reactivity :
Borreliella burgdorferi B31
application :
western blot, ELISA
more info or order :
product information
Catalog Number :
200-401-C15
Name :
Anti-OspB (RABBIT) Antibody - 200-401-C15
Display Name :
OspB Antibody
Application Note :
This protein-A purified antibody has been tested for use in Western blotting. Specific conditions for reactivity should be optimized by the user. Expect a band approximately 30.3 kDa in size corresponding to Borrelia burgdorferi OspB protein by Western blotting in the appropriate cell lysate or extract.
Buffer :
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Clonality :
Polyclonal
Concentration Value :
1.0 mg/mL
Concentration Definition :
by UV absorbance at 280 nm
Conjugation :
(None)
Size :
100 µg
Default Unit :
µg
ELISA Dilution :
1:13,000
Western Blot Dilution :
1:1,000
Expiration :
Expiration date is one (1) year from date of opening.
Format :
IgG
Gene Name :
ospB
Host Animal :
Rabbit
General Disclaimer Note :
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.
Immunogen :
MBP-fusion protein corresponding to Borrelia burgdorferi OspB protein.
Packing Type :
Ambient
Physical State :
Lyophilized
Preservative :
0.01% (w/v) Sodium Azide
Purity and Specificity :
This product was Protein-A purified and cross-adsorbed against MBP from monospecific antiserum by chromatography. This antibody is specific for Borrelia burgdorferi OspB protein. A BLAST analysis was used to suggest cross-reactivity with OspB from B. burgdorferi, afzelii, spielmanii, and garinii sources based on 100% homology with the immunizing sequence, and with B. valaisiana based on 99% homology. Cross-reactivity with OspB from other sources has not been determined.
Reconstitution Buffer :
Restore with deionized water (or equivalent)
Reconstitution Volume :
100 µL
Species Reactivity :
Borrelia burgdorferi
Storage :
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.
Synonyms :
rabbit anti-OspB Antibody, Outer surface protein B, Borrelia burgdorferi OspB, locus BB_A16
Target Species :
Borrelia burgdorferi
Background :
OspB, is one of the major Outer Surface Proteins of the outer membrane of Borrelia burgdorferi, which is composed of various unique outer surface proteins (Osp) that have been characterized (OspA through OspF). The Osp proteins are lipoproteins anchored by N-terminally attached fatty acid molecules to the membrane. They are presumed to play a role in virulence, transmission, or survival in the tick. Two of the major surface Ag of Borrelia burgdorferi, the 31-kDa OspA and 34-kDa OspB proteins, show a high degree of sequence similarity, are encoded by a 49-kb plasmid and share a common promoter, and are coordinately transcribed. OspA, OspB, and OspD are expressed by B. burgdorferi residing in the gut of unfed ticks, suggesting that they promote the persistence of the spirochete in ticks between blood meals. OspB has a contributing role in the adherence of B. burgdorferi to the tick gut. The C terminus of OspB is important for eliciting a protective immune response to OspB. B. burgdorferi has the ability to vary its surface proteins in response to immune attack.
Immunogen Type :
Recombinant Protein
Low Endotoxin :
No
Sample Size :
No
Application Text :
ELISA,Western Blot,
Other :
User Optimized
Category :
Primary Antibodies
Conjugation Name :
Unconjugated
UniProt :
P17739
NCBI :
P17739.1
Primary Image Name :
Anti-OspB Antibody - Western Blot
more info or order :
company information

Rockland Immunochemicals
321 Jones Blvd
Pottstown, PA 19464
Pottstown, PA 19464
tech@rockland.com
https://www.rockland.com/484-791-3823
headquarters: USA
Rockland Immunochemicals, Inc. produces Phosho-Site Specific Antibodies and Antibody based tools for basic, applied and clinical research. Our laboratory is located west of Philadelphia, Pennsylvania, USA. The technology base of the organization is the experience of its staff scientists in the production and purification of a wide range of antibodies through monoclonal & polyclonal antibody techniques utilizing in vitro and in vivo methods. Rockland's antibodies are suited for individuals performing Western Blotting, ELISA, Immunohistochemistry, Fluorescent Microscopy, High Content Screening and diagnostic kit production. Primary antibodies include Akt Pathway, Apolipoproteins, Apoptosis/Cell Cycle, Cytokines, Cell Signaling, Enzymes, Extracellular Matrix, Transcription Factors (NFkB) and Ubiquitin.
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