- +1 858 909 0079
- +1 858 909 0057
- [email protected]
- +1 858 909 0079
- [email protected]
Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0306 | Recombinant Protein-Ehrlichiacanis canis 28 kDa major surface antigen-1 (a.a.37 to 287) | Q9ZGJ0 | 100 µg | 1195 | |
PP0307 | Recombinant Protein-Ehrlichiacanis canis Immunodominant surface protein gp36 (a.a.20 to 287) | A9XM77 | 100 µg | 1195 | |
PP0308 | Recombinant Protein-Ehrlichiacanis canis Major P30-10 (a.a.18 to 280) | Q9F476 | 100 µg | 1195 | |
PP0309 | Recombinant Protein-Ehrlichiacanis canis Major P30 (P28-8) (a.a.20 to 288) | Q9ZGJ2 | 100 µg | 1195 | |
PP0310 | Recombinant Protein-Ehrlichiacanis canis Major P30-1 (a.a.31 to 307) | Q9ZGJ1 | 100 µg | 1195 | |
PP0311 | Recombinant Protein-Ehrlichiacanis canis Major P30-11 (a.a.30 to 279) | Q9ADV8 | 100 µg | 1195 | |
PP0312 | Recombinant Protein-Ehrlichiacanis canis Major P30-13 (a.a.46 to 278) | Q9ADW1 | 100 µg | 1195 | |
PP0313 | Recombinant Protein-Ehrlichiacanis canis Major P30-14 (a.a.20 to 289) | Q9ADW2 | 100 µg | 1195 | |
PP0314 | Recombinant Protein-Ehrlichiacanis canis Major P30-17 (a.a.18 to 316) | Q9ADW5 | 100 µg | 1195 | |
PP0315 | Recombinant Protein-Ehrlichiacanis canis Major P30-19 (a.a.37 to 296) | Q9ADW8 | 100 µg | 1195 | |
PP0316 | Recombinant Protein-Ehrlichiacanis canis Major P30-20 (a.a.33 to 275) | Q3YQQ6 | 100 µg | 1195 | |
PP0317 | Recombinant Protein-Ehrlichiacanis canis Major P30-5 (P28-1) (a.a.25 to 293) | Q9F477 | 100 µg | 1195 | |
PP0318 | Recombinant Protein-Ehrlichiacanis canis Major P30-6 (a.a.23 to 294) | Q9ADV4 | 100 µg | 1195 | |
PP0319 | Recombinant Protein-Ehrlichiacanis canis Major P30-8 (a.a.21 to 299) | Q9ADV6 | 100 µg | 1195 | |
PP0320 | Recombinant Protein-Ehrlichiacanis canis P28-9 (a.a.30 to 271) | Q9F471 | 100 µg | 1195 | |
PP0321 | Recombinant Protein-Ehrlichiacanis canisPhosphoribosylaminoimidazole carboxylase (a.a.36 to 363) | Q9AGZ2 | 100 µg | 1195 | |
PP0322 | Recombinant Protein-Ehrlichiacanis canis Preprotein translocase SecA subunit (a.a.14 to 106) | Q9ADU9 | 100 µg | 1195 | |
PP0323 | Recombinant Protein-Ehrlichiacanis canis Surface antigen D15 (a.a.18 to 418) | Q3YQW1 | 100 µg | 1195 | |
PP0324 | Recombinant Protein-Ehrlichiacanis canis Surface antigen msp4 (a.a.26 to 264) | Q3YQS4 | 100 µg | 1195 | |
PP0325 | Recombinant Protein-Ehrlichiacanis canis Surface antigen D15 (a.a.61 to 460) | Q3YQW1 | 100 µg | 1195 | |
RPP0306 | cDNA-Ehrlichiacanis canis 28 kDa major surface antigen-1 (a.a.37 to 287) | Q9ZGJ0 | 2 µg | 1250 | |
RPP0307 | cDNA-Ehrlichiacanis canis Immunodominant surface protein gp36 (a.a.20 to 287) | A9XM77 | 2 µg | 1335 | |
RPP0308 | cDNA-Ehrlichiacanis canis Major P30-10 (a.a.18 to 280) | Q9F476 | 2 µg | 1310 | |
RPP0309 | cDNA-Ehrlichiacanis canis Major P30 (P28-8) (a.a.20 to 288) | Q9ZGJ2 | 2 µg | 1340 | |
RPP0310 | cDNA-Ehrlichiacanis canis Major P30-1 (a.a.31 to 307) | Q9ZGJ1 | 2 µg | 1380 | |
RPP0311 | cDNA-Ehrlichiacanis canis Major P30-11 (a.a.30 to 279) | Q9ADV8 | 2 µg | 1245 | |
RPP0312 | cDNA-Ehrlichiacanis canis Major P30-13 (a.a.46 to 278) | Q9ADW1 | 2 µg | 1160 | |
RPP0313 | cDNA-Ehrlichiacanis canis Major P30-14 (a.a.20 to 289) | Q9ADW2 | 2 µg | 1345 | |
RPP0314 | cDNA-Ehrlichiacanis canis Major P30-17 (a.a.18 to 316) | Q9ADW5 | 2 µg | 1490 | |
RPP0315 | cDNA-Ehrlichiacanis canis Major P30-19 (a.a.37 to 296) | Q9ADW8 | 2 µg | 1295 | |
RPP0316 | cDNA-Ehrlichiacanis canis Major P30-20 (a.a.33 to 275) | Q3YQQ6 | 2 µg | 1210 | |
RPP0317 | cDNA-Ehrlichiacanis canis Major P30-5 (P28-1) (a.a.25 to 293) | Q9F477 | 2 µg | 1340 | |
RPP0318 | cDNA-Ehrlichiacanis canis Major P30-6 (a.a.23 to 294) | Q9ADV4 | 2 µg | 1355 | |
RPP0319 | cDNA-Ehrlichiacanis canis Major P30-8 (a.a.21 to 299) | Q9ADV6 | 2 µg | 1390 | |
RPP0320 | cDNA-Ehrlichiacanis canis P28-9 (a.a.30 to 271) | Q9F471 | 2 µg | 1205 | |
RPP0321 | cDNA-Ehrlichiacanis canisPhosphoribosylaminoimidazole carboxylase (a.a.36 to 363) | Q9AGZ2 | 2 µg | 1635 | |
RPP0322 | cDNA-Ehrlichiacanis canis Preprotein translocase SecA subunit (a.a.14 to 106) | Q9ADU9 | 2 µg | 800 | |
RPP0323 | cDNA-Ehrlichiacanis canis Surface antigen D15 (a.a.18 to 418) | Q3YQW1 | 2 µg | 2000 | |
RPP0324 | cDNA-Ehrlichiacanis canis Surface antigen msp4 (a.a.26 to 264) | Q3YQS4 | 2 µg | 1190 | |
RPP0325 | cDNA-Ehrlichiacanis canis Surface antigen D15 (a.a.61 to 460) | Q3YQW1 | 2 µg | 1995 |
Ehrlichiacanis canis cDNA and recombinant antigen
Ehrlichiacanis canis is a species of gram-negative obligate intracellular bacteria that is the causative agent of canine ehrlichiosis. It is transmitted to dogs by bites from infected brown dog ticks and can cause a variety of symptoms ranging from fever, anemia, and lymphadenopathy, to depression, lameness, and even death. The diagnosis of E. canis infection is typically made by looking for the presence of the organism’s antigen in the blood. This is done through a serologic test, such as the indirect fluorescent antibody test, or the enzyme-linked immunosorbent assay.Several proteins have been identified in Ehrlichiacanis canis, which play a crucial role in the pathogenesis of the disease.
One of the most important proteins is the 28 kDa major surface antigen 1, which is responsible for the attachment of the bacteria to the host cells. This protein is also considered a potential vaccine candidate against ehrlichiosis.
Another significant protein is the immunodominant surface protein gp36, which is involved in the binding of the bacteria to the host cells and helps in the establishment of infection. The major P30 proteins (P30-10, P30, P30-1, P30-11, P30-13, P30-14, P30-17, P30-19, P30-20, P30-5, P30-6, and P30-8) are known to play a role in antigenicity and are potential targets for diagnostic tests.
The lipoprotein antigen P28-9 is involved in the stimulation of the host immune system and may be considered as a potential vaccine candidate. Phosphoribosylaminoimidazole carboxylase, Preprotein translocase SecA subunit, and surface antigen D15 are also potential vaccine candidates against ehrlichiosis.
The surface antigen msp4 is involved in the attachment of the bacteria to host cells and helps in the establishment of the infection. The surface antigen D15 is involved in the survival and replication of the bacteria inside the host cells.
Overall, these proteins play a critical role in the pathogenesis of ehrlichiosis and provide potential targets for the development of vaccines and diagnostic tests against the disease.
The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.
Ehrlichiacanis canis cDNA and recombinant antigen can be used in ELISA (Enzyme-Linked ImmunoSorbent Assay) to detect E. canis infection in dogs. Using cDNA and recombinant antigen, researchers can develop an ELISA test that is sensitive and specific for the detection of E. canis antibodies. The ELISA test can be used to test for the presence of E. canis antibodies in canine serum or other bodily fluids. The test will detect antibodies to the E. canis antigen, which will indicate that the dog has been exposed to E. canis and may be infected with the pathogen.
Get the Latest News and Updates by Email
6393 Nancy Ridge Dr. Suite A
San Diego, CA 92121 USA
Fax: +1-858-909-0057
Get the Latest News and Updates by Email
© 2023 Bioclone Inc. All Rights Reserved.
Magnetic Beads Make Things Simple