Production of Recombinant Proteins

Expect the fastest turnaround time when working with us

Novatein Biosciences offers recombinant protein production services to accelerate your research and development, by using highly efficient recombinant protein expression strategies. A general outline of our protein production service is as follows:

1. PCR amplification: Customer provides the accession number of the target gene. We will design the primers and amplify it from the target cells using high fidelity PCR.

2. Gene cloning: The PCR amplified gene will be cloned into a plasmid vector and the sequence is authenticated by DNA sequencing.

3. Gene expression: Based on the customer request, the target gene will be cloned into bacterial/ yeast/ baculoviral or mammalian expression vectors with or without a tag.


Protein Services

4. Protein Purification: The protein will be purified by column chromatography procedures (affinity and gel filtration).

5. Protein Identification: The purified protein will be separated on SDS-PAGE gel and stained/ transferred to membrane for immunoblot. Mass spectrometry can be performed for an additional charge.

Note: For most of the eukaryotic protein production, baculovirus expression system is the first line of choice due to high yield and posttranslational modifications. If the protein activity is dependent on the posttranslational modifications, the mammalian expression system is the choice.

Protein Expression and Purification Service (Analytical to preparative amounts of proteins)

Novatein Biosciences has extensive experience in the recombinant protein expression and purification. Express your proteins with or without tags in

  • Bacterial cells: various strains
  • Yeast cells: Pichia, Saccharomyces
  • Insect cells : S2, Sf9, Sf21, and Hi5 cells
  • Mammalian cells: CHO, HEK293 and others

With our over a decade years of experience, we are experts in creating and optimizing stable and transient expression for secreted or intracellular, cytosolic or periplasmic, tagged or untagged proteins. We assess expression levels using the SDS-PAGE, Western, ELISA or functional analysis. We optimize protein expression by modification of, promoter, ribosome binding site, vector copy number, host cell, growth condition including media and additives, time, and temperature

In addition, we offer the following services:

  • Stable isotopic labeling
  • Inclusion body purification
  • Refolding with typical or preferred protocols

For protein purification, we have the capability to run the following:

  • Affinity Chromatography
  • Ni- NTA, Talon resins, Glutathione Sepharose, Heparin Sepharose, Streptavidin Sepharose, and anti-Flag
  • Ion Exchange Chromatography
  • Mono-Q, Q Sepharose Fast Flow, Resource Q, Q Sepharose XL, ANX, DEAE Sepharose, SP Sepharose, CM Sepharose
  • Hydrophobic interaction Chromatography
  • Phenyl and (CH2)n Sepharose
  • Immuno-Affinity Chromatography
  • Protein A and Protein G Sepharose
  • Size Exclusion Chromatography

Fc Fusion Protein Production and Purification Services

Novatein Biosciences has extensive experience in the expression and purification of a number of Fc fusion proteins from microgram to kilogram scales in CHO and HEK 293 cells. Using our proprietary fully optimized secretion signal and linker sequences, we can efficiently complete a project from gene construction to Fc fusion protein purification. Fc fusion can be N-terminal or C-terminal. Multiple Fc backbones are available to choose from.

Fast turnaround:

1-2 weeks for codon optimization and synthesizing the gene of interest.

1-2 weeks for molecular construction of recombinant Fc fusion proteins using E.coli.

Protein A is used for recombinant antibody purification. Please request if multiple purification methods are required.

Recombinant Protein Production Using the Insect Cell Expression System

Gene of interest (GOI) is cloned into a suitable donor plasmid containing a mini-Tn7 element.

The recombinant donor plasmid is then transformed into E. coli cells which contain abacmid with a mini-attTn7 target site and a helper plasmid. The mini-Tn7 element on the donor plasmid facilitates transposition of the GOI into the target site on the bacmid resulting in insertion of the GOI into the bacmid DNA.

Recombinant bacmid DNA is extracted and purified (for efficient homologous recombination, pure DNA is required).

Insect cells are transfected with the recombinant bacmid DNA to produce recombinant baculovirus particles with GOI (P1 virus generation).

The infectious potency of P1 baculovirus is determined by plaque assay (site specific transposition does not require P1 viral particles purification)

The insect cell cultures are infected with the purified P1 stock to create a P2 stock (100 ml serum free medium).
A high quality high titer working virus stock P3 (~500 ml) is produced by infecting Sf9 cells with a P2 virus at a low multiplicity of infection (MOI=0.1)
Optimization of heterologous protein expression and purification of protein by successive chromatography techniques


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