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Tag-free Recombinant Protein Production

$7,950.00$12,050.00

Antibody: Monoclonal Antibody

Concentration: 1 mg/ml of purified protein

Application: Recombinant Protein Expression

Reactivity: Human, Insect, Yeast

BiCell Scientific Inc has developed a robust protein expression system utilizing monoclonal antibody to purify recombinant proteins from a variety of model cells.

Current lab practice for purifying recombinant protein is by using various protein/peptide tags, such as poly-His tag, Flag tag, GST tag and etc. While these tags allow rapid affinity purification with existing substrates, the tags, themselves, may alter the structure and function of recombinant proteins. It is therefore highly recommended that no tag is used on recombinant protein for high-end applications, such as protein crystallization or cryoEM, protein therapeutics, protein biologics and etc.

BiCell Scientific Inc has developed a robust protein expression system utilizing monoclonal antibody to purify recombinant proteins from a variety of model cells, e.g. human HEK293 cells or industrial-grade CHO cells, insect Sf9 cells and yeast Pichia pastoris cells. In addition to purified proteins, customers will receive one or two monoclonal antibodies that have been validated by affinity chromatography and can be used for future affinity purification.

BiCell Scientific’s single mAb column is able to achieve target protein purity of >80%; dual mAb column (sequential) is able to achieve purity of >95%. Final protein product is separated by gel filtration column and stained in Coomassie blue gel as single band.

Recombinant Protein Workflow Chart

Steps Timeline (weeks) Deliverables/Internal testing milestone QC standard
Phase I: Monoclonal antibody generation

(one or two epitopes, 13-19 aa long, selected from different regions of target protein will be used to generate mouse monoclonal antibody)

3-4 months 1 mg mAb IgG ELISA

 

 

 

 

Phase II: Recombinant protein expression

(cDNA encoding target protein will be cloned into lentivirus, baculovirus or yeast targeting vector to generate stable expression system in HEK293 or CHO cells, Sf9 cells or Pichia yeast, respectively)

 

 

1-2 months / Western blot
Phase III: Recombinant protein purification

(one or two monoclonal antibodies will be conjugated to Sepharose column for affinity purification of target protein; purified protein will be further separated by gel filtration column to ensure purity)

 

 

1-2 months 1 mg recombinant protein (guaranteed purity after gel filtration column) Coomassie blue gel

 


For Research Use Only. Not for use in clinical diagnostics.

  • One or two mAb frozen clones and purified IgG (1 mg)
  • Affinity purified recombinant protein (1 mg)
  • Model cells stably expressing recombinant protein (frozen HEK293 or CHO or Sf9 or Pichia yeast, 1×106 cells)

Additional information

Protein Expression System

Industrial-grade CHO cell, Human HEK293 cell, Insect Sf9 cell, Yeast Pichia pastoris

Antibody Purification System

Single mAb column, Dual mAb column

Reviews

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Be the first to review “Tag-free Recombinant Protein Production”

"I am really impressed with your approach. We tried multiple times previously to create monoclonal and polyclonal antibodies to claudin-2 and MLCK1. We have had limited success generating polyclonals and no success generating monoclonals. You have generated outstanding monoclonals to both. I look forward to continuing to work with you."

Jerrold R. Turner, M.D., Ph.D.

Brigham and Women’s Hospital | Harvard Medical School

"The polyclonal antibody you generated for KIAA0408 is stunning! KIAA0408 is a novel cilium molecule that has never been studied. So, clearly there will be a lot of demand for it as we have discovered a very interesting finding and the story will be published in a high impact journal. I am strongly inclined to generate monoclonal antibody for this protein too and we should think about patenting it."

Univ.-Prof. Jay Gopalakrishnan PhD

Heinrich-Heine-Universität | Universitätsklinikum Düsseldorf

"Your ARL13B antibody works beautifully!!! We’re so happy to have a cilia-specific antibody made in rat! I can send you high resolution images to be posted on your website."

Julie Craft Van De Weghe, PhD

School of Medicine | University of Washington

"The assay is a homophilic interaction mediated cell adhesion on purified protein (in this case, immobilized purified Pcdhga9 to Pcdhga9 expressed on cell surface). Compared to control, cell adhesion is reduced in the presence of Pcdhga9 monoclonal antibody supernatants!"

Divyesh Joshi, PhD

School of Medicine | Yale University

"The rabbit hybridoma supernatants of anti-APOBEC3 project are tested positive by ELISA, and we are very happy about it! We previously tried a company, Abclone. Their Project "A" has immune response that is <10,000 titer in antiserum, which would explain why there is no positive mAb after fusion. Their project "B" didn't have any immune response in rabbit."

Harshita B Gupta, PhD.

School of Medicine | UT Health San Antonio

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