Plant Protein Expression and Purification Services

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Plant Protein Expression and Purification Services

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CD BioSciences provides prokaryotic, yeast, insect cell, and mammalian cell expression systems with various bioreactor sizes to meet multiple expression requirements. We can also perform protein isolation and purification simultaneously, saving clients research time.

Overview of protein production and characterization.  Figure 1. Overview of protein production and characterization. (Wingfield P. T. 2015)

Proteins are involved in plant growth, development, heredity, and reproduction. Studying the phenomenon and essence of plant life activities from the perspective of proteins can grasp the law of its activities more scientifically and reveal its molecular biology mechanism more perfectly. Therefore, many scholars have focused research in the field of life science on proteins. Obtaining high-quality, high-purity, and high natural fidelity proteins is a crucial first step.

Service Content

Plant Complex Proteins Expression and Purification Services

Complex proteins we can prepare including
Plant glycosylated protein Plant disulfide protein Plant kinase
Plant toxic protein Plant membrane protein

Plant Protein Large-Scale Expression and Purification Service

Service Details

Tag selection service

We provide expression tags such as

  • His-tag (histidine tag)
  • GST-tag (glutathione sulfotransferase tag)
  • MBP-tag (maltose-binding protein tag)
  • CBD-tag (chitin-binding region tag)

We select suitable tags for clients according to the characteristics of the protein, the molecular weight of the tag, the ability to regulate the solubility of the protein, the effect on protein folding, and whether it needs to be excised.

Vector construction service

We provide clients with the service of constructing expression vectors and offer commercialized vectors for choice, such as pET28 series with His-tag, pMAL series with MBP-tag, etc.

Host selection service

Expression systems Feature
E. coli
  • Low cost, rapid expression, easy to scale up, and most widely used.
  • Not easily post-translationally modified and forms inclusion bodies.
  • Difficult to express higher MW proteins.
Yeast
  • Completion of partial post-translational modifications.
  • Unique glycosylation pattern with high mannose content in glycans.
Baculovirus-Insect cells
  • Desirable post-translational modifications and easy to scale up.
  • High cell density for soluble protein production, suitable for toxic proteins.
  • More demanding cultural conditions.
  • Lack of partial glycosylation and high cost.
Mammalian cells
  • Produces soluble proteins with lower endotoxins and better biological activity.
  • Comprehensive post-translational modifications.
  • Transient and stable expression.
  • Produces recombinant antibodies or antibody fragments.

Purification method selection service

Our methods
Gel filtration chromatography Reversible conjugation
Ion exchange chromatography Thermal stability differential separation
Affinity chromatography Solubility differential separation
Hydrophobic interaction chromatography Proteolytic impurities

The Client Provides

Target gene sequence information

Target gene template plasmid

Template plasmid resistance information

Deliverables

Recombinant Plasmids

Sequencing Report

SDS-PAGE assay

Pure protein in the amount required by the client

CD BioSciences is a biological company specializing in plant proteins. We offer tailored solutions to meet clients' unique needs, providing high-quality protein expression and purification for scientific research. We specialize in optimizing expression systems and purification technologies to ensure the highest purity and production of target proteins. Please contact us for your plant protein preparation needs and we will help you unlock the full potential of plant proteins to accelerate your scientific discoveries.

References

  1. Yesilirmak, F., & Sayers, Z. (2009). Heterologous expression of plant genes. International journal of plant genomics. 2009:296482.
  2. Wingfield P. T. (2015). Overview of the purification of recombinant proteins. Current protocols in protein science, 80:6.1.1–6.1.35.

For research use only, not for clinical use.