Products

Acinetobacter baumannii cDNA and Antigen

Cat#

Product Name

Swiss Prot#

Size

Price (US$)

Order

PP0001

Recombinant Protein-Acinetobacter baumannii 17 kDa surface antigen (a.a.21 to 209)

B7IB53

100 µg

1195

Order

PP0002

Recombinant Protein-Acinetobacter baumannii Epstein-Barr nuclear antigen 1 EBV nuclear antigen 1 EBNA-1 (a.a.21 to 121)

B7H1J6

100 µg

1195

Order

PP0003

Recombinant Protein-Acinetobacter baumannii Major membrane protein I MMP-I antigen (a.a.31 to 310)

B0VBK0

100 µg

1195

Order

PP0004

Recombinant Protein-Acinetobacter baumannii A 190 kDa antigen (a.a.61 to 420)

B7GW41

100 µg

1195

Order

PP0005

Recombinant Protein-Acinetobacter baumannii Rickettsia 17 kDa surface antigen (a.a.27 to 140)

B7H0L6

100 µg

1195

Order

PP0006

Recombinant Protein-Acinetobacter baumannii Surface antigen (a.a.61 to 460)

B7H123

100 µg

1195

Order

RPP0001

cDNA-Acinetobacter baumannii 17 kDa surface antigen (a.a.21 to 209)

B7IB53

2 µg

940

Order

RPP0002

cDNA-Acinetobacter baumannii Epstein-Barr nuclear antigen 1 EBV nuclear antigen 1 EBNA-1 (a.a.21 to 121)

B7H1J6

2 µg

800

Order

RPP0003

cDNA-Acinetobacter baumannii Major membrane protein I MMP-I antigen (a.a.31 to 310)

B0VBK0

2 µg

1395

Order

RPP0004

cDNA-Acinetobacter baumannii A 190 kDa antigen (a.a.61 to 420)

B7GW41

2 µg

1795

Order

RPP0005

cDNA-Acinetobacter baumannii Rickettsia 17 kDa surface antigen (a.a.27 to 140)

B7H0L6

2 µg

800

Order

RPP0006

cDNA-Acinetobacter baumannii Surface antigen (a.a.61 to 460)

B7H123

2 µg

1995

Order

Acinetobacter baumannii 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

Acinetobacter baumannii is a species of Gram-negative bacteria that is commonly found in soil and water. It is also a significant human pathogen that can cause a range of infections, including pneumonia, bloodstream infections, urinary tract infections, and wound infections.

Acinetobacter baumannii is a gram-negative bacterium that is becoming increasingly resistant to antibiotics, making it a significant threat to public health. One of the key antigens associated with this bacterium is the 17 kDa surface antigen, which plays a role in the bacterium’s ability to adhere to and invade host cells.

Another key antigen associated with Acinetobacter baumannii is the Major membrane protein I (MMP-I) antigen. This protein is involved in the bacterium’s ability to adhere to and invade host cells, and it is also a target for the host’s immune response.

The A 190 kDa antigen is another important antigen associated with Acinetobacter baumannii. This protein is involved in the bacterium’s ability to form biofilms, which can protect the bacterium from antibiotics and the host’s immune system.


In addition to these antigens, surface antigens are also important components of these bacteria and viruses. Surface antigens are involved in the bacterium’s or virus’s ability to interact with the host’s immune system, and they can be important targets for the development of vaccines and therapeutics.

Bioclone’s proprietary technology platform offers a solution to the challenges faced in heterologous expression systems, unlocking the full potential of recombinant proteins. With over 6,000 artificially synthesized codon-optimized cDNA clones, researchers can enjoy increased expression levels and better research outcomes. Whether for academic research or therapeutic applications, Bioclone’s technology is a valuable tool for maximizing the production of recombinant proteins.

The use of recombinant proteins and cDNA in academic research and therapeutic applications has experienced substantial growth. However, the success of heterologous expression systems largely depends on various factors, such as codon preference, RNA secondary structure, and GC content.

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