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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 human Talin-1 protein CSB-RP051844h 1mg
    Recombinant Lassa virus Pre-glycoprotein polyprotein GP complex(GPC), partial CSB-YP362480LNP1 1mg
    Recombinant Macaca fascicularis UDP-glucuronosyltransferase 2B9(UGT2B9) ,partial CSB-YP520775MOV1 1mg
    Recombinant Human Adenosine receptor A2a(ADORA2A),partial CSB-YP001376HU 1mg
    Recombinant Human Bombesin receptor subtype-3(BRS3),partial CSB-YP002820HU1 1mg
    Recombinant Human Sarcoplasmic/endoplasmic reticulum calcium ATPase 2(ATP2A2) ,partial CSB-YP002333HU 1mg
    Recombinant Human ATP-binding cassette sub-family G member 1(ABCG1), partial CSB-YP001080HU1 1mg
    Recombinant Homo sapiens (Human) Vasohibin-2,E.coli CSB-EP769783HU 1mg/500ug/200ug/50ug/10ug
    Recombinant Orientia tsutsugamushi 56 kDa type-specific antigen, partial CSB-YP327749OCJ1 1mg
    Recombinant Saccharomyces cerevisiae Inositol phosphorylceramide synthase catalytic subunit AUR1(AUR1), partial CSB-YP334079SVG1 1mg
    Recombinant human 78 kDa glucose-regulated protein CSB-RP050294h 1mg
    Recombinant Human respiratory syncytial virus B Fusion glycoprotein F0(F) ,partial, Mammalian cell CSB-MP516611HXK 1mg/500ug/100ug/50ug
    Recombinant Human respiratory syncytial virus B Fusion glycoprotein F0(F) ,partial, Baculovirus CSB-BP516611HXK 1mg/500ug/100ug/50ug
    Recombinant Human respiratory syncytial virus B Fusion glycoprotein F0(F) ,partial, Escherichia Coli CSB-EP516611HXK 1mg/500ug
    Recombinant rabbit Fructose-bisphosphate aldolase B, Mammalian cell CSB-MP001586RB 1mg/500ug/100ug/50ug
    Recombinant rabbit Fructose-bisphosphate aldolase B, Baculovirus CSB-BP001586RB 1mg/500ug/100ug/50ug
    Recombinant human HLA class I histocompatibility antigen, alpha chain G protein, Escherichia Coli CSB-EP010509HU 1mg/500ug
    Recombinant human HLA class I histocompatibility antigen, alpha chain G protein, Baculovirus CSB-BP010509HU 1mg/500ug/100ug/50ug
    Recombinant Human Galectin-9(LGALS9), Baculovirus CSB-BP012895HU 1mg/500ug/100ug/50ug
    Recombinant Hepatitus C virus Genome Polyprotien, Baculovirus CSB-BP313207HJD(A4) 1mg/500ug/100ug/50ug

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