Products

Crithidia fasciculata cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0149

Recombinant protein-Crithidia fasciculata CACK protein (a.a.30 to 316)

O61129

100 µg

1195

Order

RPL0149

cDNA-Crithidia fasciculata CACK protein (a.a.30 to 316)

O61129

2 µg

1716

Order

Crithidia fasciculata 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

Crithidia fasciculata is a flagellated protozoan parasite that infects insects and other invertebrates. This parasite is commonly used in research as a model organism for studying various biological processes.

The CACK protein is a key antigen associated with Crithidia fasciculata. This protein is a component of the kinetoplast, which is a unique organelle found in the mitochondria of trypanosomatid parasites such as Crithidia fasciculata. The CACK protein is involved in the regulation of mitochondrial DNA replication and is essential for the survival of the parasite.

Understanding the function and interaction of the CACK protein is crucial for the development of effective diagnostic tests and vaccines to prevent and control the spread of Crithidia fasciculata infections. Further research on this antigen could potentially lead to the development of new treatment options for Crithidia fasciculata infections, as well as for other trypanosomatid parasites.

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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