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Protein

Protein

CusAb Protein Expression Platform has established five recombinant expression systems from prokaryotic to eukaryotic, and has also built cell-free expression system. We own protein expression technology based on a series of protein expression and purification technology, including protein expression technology shown by Baculovirus outer membrane proteins (OMP), and membrane protein expression technology, etc., and we have the ability to make a variety of difficult proteins. The recombinant proteins we provide include cytokines, hormones, enzymes, viral antigens, allergens, human disease-related proteins, and animal and plant and microbial proteins, etc., of which there are 327 kinds of active proteins.

The Characteristics of Five Expression Systems

Escherichia coli (E.coli) expression system Advantages
  • 1.

    Clear genetic background;

  • 2.

    Low cost and simple culture conditions;

  • 3.

    Simple transformation operation;

  • 4.

    Short protein expression period;

  • 5.

    High rate of reproduction and expression level;

  • 6.

    A variety of carriers and fusion tags to choose;

  • 7.

    Many parameters can be altered to optimize expression.

  • 8.

    Tag can be available at both N-terminal and C-terminal with an enzyme cutting site that is easy to cut.

Disadvantages
  • 1.

    Inefficient disulfide bond formation and poor folding lead to inclusion body formation;

  • 2.

    Poor post-translational modifications (such as glycosylation, alkylation, phosphorylation, specificity of proteolytic processing, etc.);

  • 3.

    The success rate and recovery rate of inclusion body renaturation is not very high.

Applications Purified protein (structure, enzymology, drug discovery);
Protein therapeutics.
Pichia pastoris (Yeast) expression system Advantages
  • 1.

    Low cost and high expression level;

  • 2.

    Self-produced Endotoxin-free;

  • 3.

    Efficient protein folding and secretory expression;

  • 4.

    Simple culture conditions and purification operation;

  • 5.

    Extensive post-translational modifications: Glycosylation, phosphorylation, acyl lipid;

  • 6.

    Can develop high density fermentation by using simple inorganic salt, large biomass;

  • 7.

    The protein is more stable than the prokaryotic expression, and is especially suitable for the expression of eukaryotic genes and the preparation of functional expression proteins;

  • 8.

    Simple laboratory and industrial operation.

Disadvantages
  • 1.

    Glycosylation modification is not good as mammalian cells.

Applications Purified protein (structure, enzymology, drug discovery).
Baculovirus-infected insect cells expression system Advantages
  • 1.

    Good expression levels and relatively rapid growth;

  • 2.

    More advantages over the expression of viral proteins;

  • 3.

    Glycosylation modification more like mammalian cells;

  • 4.

    Relatively de-glycosylation modification (good for structure determination);

  • 5.

    Large gene volume: because the baculovirus genome is larger, so it can carry large gene fragment;

  • 6.

    High security: the baculovirus has a strict species specificity, not infected with vertebrates and plants;

  • 7.

    High expression efficiency of exogenous gene: compared with other eukaryotic expression systems, the baculovirus system can efficiently express exogenous protein from infected cells;

  • 8.

    The expression product has high activity: baculovirus will proliferation in insect host cells, thus resulting recombinant protein will be similar to mammalian cells in post-translational modification, the expression product has a strong biological activity;

  • 9.

    Easy to amplify: baculovirus can mass production of recombinant protein products with biological activity.

Disadvantages
  • 1.

    Expensive culture media cost;

  • 2.

    Inefficient processing of pro-peptides in secretory pathway;

  • 3.

    Viral infection leads to cell lysis and potential degradation of expressed proteins;

  • 4.

    Glycosylation modification is not good as mammalian cells.

Applications Purified protein (structure, enzymology, drug discovery).
Mammalian cells expression system Advantages
  • 1.

    Self-produced Endotoxin-free;

  • 2.

    Efficient protein folding and secretory expression;

  • 3.

    All post-translational modifications, provide a variety of complex N glycosylation and accurate O type glycosylation and other post-translational processing functions;

  • 4.

    The expressed products are closest to the natural biological proteins in molecular structure, physical and chemical properties and biological functions.

Disadvantages
  • 1.

    Expensive culture media cost;

  • 2.

    Complex growth requirements.

Applications Purified protein (structure, enzymology, drug discovery);
Protein therapeutics;
Cell-based studies.
Cell-free expression system Advantages
  • 1.

    High expression level: we provide the original and optimized pET carrier with a series of labels, so that the membrane protein yield can reach mg grade;

  • 2.

    Protein synthesis conditions can be manipulated;

  • 3.

    The target fusion protein with 6*His is beneficial to the purification.

Disadvantages
  • 1.

    Limited post-translational modifications;

  • 2.

    Expensive for scale-up.

Applications Purified protein (structure, enzymology, drug discovery);
In vitro expression cloning;
Isotopic labelling of proteins for NMR;
Incorporation of non-natural amino acids.

Protein

Advanced Search

  • Product Name Code Size
    Recombinant Pig Growth hormone-releasing hormone receptor(GHRHR), partial CSB-YP009413PI1 1mg
    Recombinant Rat Sterol regulatory element-binding protein 1(Srebf1), partial CSB-YP022657RA1 1mg
    Recombinant Autographa californica nuclear polyhedrosis virus Major envelope glycoprotein(GP67) ,partial CSB-YP324635ARA1 1mg
    Recombinant Human Orexin receptor type 1(HCRTR1), partial CSB-YP010231HU1 1mg
    Recombinant Mouse Aquaporin-4(Aqp4), partial CSB-YP001964MO1 1mg
    Recombinant Virulence sensor protein BvgS(bvgS) ,partial CSB-YP336705BIK 1mg
    Recombinant Pan troglodytes C-C chemokine receptor type 5(CCR5), partial CSB-YP004844EQV1 1mg
    Recombinant Rat Muscarinic acetylcholine receptor M5(Chrm5), partial CSB-YP005385RA1 1mg
    Recombinant Human POU domain, class 5, transcription factor 1(Pou5f1) CSB-MP018403HU 1mg/500ug/100ug/50ug
    Recombinant Human POU domain, class 5, transcription factor 1(Pou5f1) CSB-BP018403HU 1mg/500ug/100ug/50ug
    Recombinant Human POU domain, class 5, transcription factor 1(Pou5f1) CSB-EP018403HU 1mg/500ug/100ug/50ug
    Recombinant Human POU domain, class 5, transcription factor 1(Pou5f1) CSB-YP018403HU 1mg/500ug
    Recombinant Rhodopseudomonas palustris Aquaporin Z(aqpZ), partial CSB-YP351570RLU1 1mg
    Recombinant Human Frizzled-7(FZD7), partial CSB-YP009110HU1 1mg
    Recombinant Aquaporin Z(aqpZ), partial CSB-YP524789SZB1 1mg
    Recombinant Human CD97 antigen(CD97), partial CSB-YP004972HU1 1mg
    Recombinant Mouse High affinity immunoglobulin epsilon receptor subunit beta(Ms4a2), partial CSB-YP015013MO1 1mg
    Recombinant Mouse Interleukin-18(Il18) CSB-YP011608MO 1mg
    Recombinant Cricetulus griseus Serine palmitoyltransferase 2(SPTLC2) ,partial CSB-YP022640DXU1 1mg
    Recombinant Saccharomyces cerevisiae GPI-anchored wall transfer protein 1(GWT1), partial CSB-YP343629SVG 1mg

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