Products

Rickettsia Felis cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0656

Recombinant protein-Rickettsia Felis Cell surface antigen-like protein Sca8 (a.a.61 to 460)

Q4UKK8

100 µg

1195

Order

PL0657

Recombinant protein-Rickettsia Felis Cell surface antigen-like protein Sca12 (a.a.61 to 476)

Q4UJI1

100 µg

1195

Order

PL0658

Recombinant protein-Rickettsia Felis Cell surface antigen-like protein Sca7 (a.a.18 to 103)

Q4UM88

100 µg

1195

Order

PL0659

Recombinant protein-Rickettsia Felis O-antigen export system permease protein RfbA (a.a.60 to 258)

Q4UNK2

100 µg

1195

Order

PL0660

Recombinant protein-Rickettsia Felis Cell surface antigen-like protein Sca13 (a.a.61 to 460)

Q4UJZ8

100 µg

1195

Order

PL0661

Recombinant protein-Rickettsia Felis Cell surface antigen Sca3 (a.a.61 to 460)

Q4ULM9

100 µg

1195

Order

PL0662

Recombinant protein-Rickettsia Felis 17 kDa surface antigen (a.a.21 to 159)

Q9F9F2

100 µg

1195

Order

PL0663

Recombinant protein-Rickettsia Felis Cell surface antigen-like protein Sca10 (a.a.18 to 107)

Q4UNF9

100 µg

1195

Order

PL0664

Recombinant protein-Rickettsia Felis surface cell antigen sca1 (a.a.61 to 460)

Q4UNI5

100 µg

1195

Order

PL0665

Recombinant protein-Rickettsia Felis Cell surface antigen-like protein Sca11 (a.a.31 to 333)

Q4UMN8

100 µg

1195

Order

PL0666

Recombinant protein-Rickettsia Felis polysaccharide polymerase RF_0568 (a.a.20 to 407)

Q4UM04

100 µg

1195

Order

PL0667

Recombinant protein-Rickettsia Felis Antigenic heat-stable 120 kDa protein (a.a.61 to 460)

Q9AJ37

100 µg

1195

Order

PL0668

Recombinant protein-Rickettsia Felis surface cell antigen sca2 (a.a.61 to 460)

Q4UNE0

100 µg

1195

Order

PL0669

Recombinant protein-Rickettsia Felis O-antigen export system ATP-binding protein RfbE (a.a.21 to 247)

Q4UNK1

100 µg

1195

Order

PL0670

Recombinant protein-Rickettsia Felis Cell surface antigen-like protein Sca9 (a.a.61 to 460)

Q4UJZ7

100 µg

1195

Order

RPL0656

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca8 (a.a.61 to 460)

Q4UKK8

2 µg

2394

Order

RPL0657

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca12 (a.a.61 to 476)

Q4UJI1

2 µg

2490

Order

RPL0658

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca7 (a.a.18 to 103)

Q4UM88

2 µg

510

Order

RPL0659

cDNA-Rickettsia Felis O-antigen export system permease protein RfbA (a.a.60 to 258)

Q4UNK2

2 µg

1188

Order

RPL0660

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca13 (a.a.61 to 460)

Q4UJZ8

2 µg

2394

Order

RPL0661

cDNA-Rickettsia Felis Cell surface antigen Sca3 (a.a.61 to 460)

Q4ULM9

2 µg

2394

Order

RPL0662

cDNA-Rickettsia Felis 17 kDa surface antigen (a.a.21 to 159)

Q9F9F2

2 µg

828

Order

RPL0663

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca10 (a.a.18 to 107)

Q4UNF9

2 µg

800

Order

RPL0664

cDNA-Rickettsia Felis surface cell antigen sca1 (a.a.61 to 460)

Q4UNI5

2 µg

2394

Order

RPL0665

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca11 (a.a.31 to 333)

Q4UMN8

2 µg

1812

Order

RPL0666

cDNA-Rickettsia Felis polysaccharide polymerase RF_0568 (a.a.20 to 407)

Q4UM04

2 µg

2322

Order

RPL0667

cDNA-Rickettsia Felis Antigenic heat-stable 120 kDa protein (a.a.61 to 460)

Q9AJ37

2 µg

2394

Order

RPL0668

cDNA-Rickettsia Felis surface cell antigen sca2 (a.a.61 to 460)

Q4UNE0

2 µg

2394

Order

RPL0669

cDNA-Rickettsia Felis O-antigen export system ATP-binding protein RfbE (a.a.21 to 247)

Q4UNK1

2 µg

1356

Order

RPL0670

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca9 (a.a.61 to 460)

Q4UJZ7

2 µg

2394

Order

RPL0656

cDNA-Rickettsia Felis Cell surface antigen-like protein Sca8 (a.a.61 to 460)

Q4UKK8

2 µg

2394

Order

Rickettsia Felis cDNA and recombinant antigen

  • Codon-optimized cDNA is cloned into E. coli expression vector with 6x His-tag at N-terminus and ready-to-use for recombinant protein production.
  • Recombinant protein applications: Western Blot may be used for other applications determined by the user.
  • Protein Purity: >90%, as determined by SDS-PAGE under reducing conditions.
  • Protein Activity: N/A
  • Protein Tag:  Contains A 6x histidine tag at N-terminus.
  • Protein Formulation: Liquid
  • Source: Produced from E. coli

Rickettsia Felis is a bacterium that is an obligate intracellular parasite of eukaryotic cells. It is the most common cause of spotted fever rickettsiosis in humans and is found throughout the world. The antigen of Rickettsia Felis is a protein-based molecule, which is composed of several proteins, such as rickettsial surface antigens (RSA), outer membrane proteins (OMP), and lipopolysaccharide (LPS). The antigen is used to produce antibodies, which can be used to diagnose spotted fever rickettsiosis. Additionally, the antigen can also be used to develop vaccines against the disease.

17 kDa surface antigen: Presence in other Rickettsia species
Role in bacterial pathogenesis
Antibody response to 17 kDa surface antigen

RF_0568: Localization on the surface of Rickettsia Felis
Importance in bacterial pathogenesis
Conservation among Rickettsia specie

120 kDa protein: Role in bacterial adherence and invasion
Antibody response to 120 kDa protein
Potential as a vaccine target


Rickettsia Felis cDNA and recombinant antigens are used in molecular diagnostics for the detection and/or identification of R. Felis infection. The cDNA has been used to detect R. Felis genes in a variety of biological samples, including blood and tissue samples. The recombinant antigen can be used for the serological detection of R. Felis antibodies in human and animal sera. Additionally, both cDNA and recombinant antigens can be used to develop rapid, sensitive, and specific detection assays for R. Felis.

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.

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