Sometimes, we also use BCA method.
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All of our proteins are purified under mild conditions. If a protein we provide is full length of mature protein, then it should have activity in theory. If the protein is active after their validation, they could purchase larger size later, and we will provide certain discount for their re-order.
We also have some proteins that have been verified for their activity and we have listed their biological activity data on our website. Click here to learn more about corresponding protein for details. Additionally, we have good capacity and experience for large-scale expression 10 mg, 50 mg, mg, mg, mg, etc. Sometimes, the tag of proteins will be determined during the manufacturing process.
If you have specified tag type, please feel free to consult with us. Click here to learn more about the general information of different tags. Theoretically small tags generally have very small influence on protein activity. However, the specific impact on protein activity can't be concluded There is no impact on some proteins, small impact on some proteins, and relatively great impact on some proteins.
Not all protein tags can be removed as some proteins will be very unstable after tag removal. Please communicate with us in advance if you need to remove the tag which takes business days. If we succeed in removing the tag, we will charge for extra cost for tag removal. If we fail in removing the tag, we won't charge for any extra cost, and remark this information in datasheet as follows "Note: The laboratory determined that the tag on your protein could not be removed with standard laboratory procedures.
Your protein is being supplied with the tag intact. Not all endotoxin can be removed. We could offer endotoxin removal service free of charge using PMB affinity chromatography, use LAL reagent to semi-quantitatively detect the content of endotoxin and guarantee endotoxin level within 0. Yes, we can offer this service and it is free of charge, but you should remark this information when placing the order.
We've performed aseptic processing for liquid protein before lyophilization, but there may exist contamination during lyophilization process, so we can't say germ-free for the whole process.
We could provide corresponding antibody for the recombinant protein. Based on the quotation for the recombinant protein, add certain cost, we will offer mg affinity-purified polyclonal antibody with a guarantee of western blot and ELISA positive on this recombinant protein.
The delivery time will be 2. Please feel free to contact us to get more details. CUSABIO protein product does not contain carrier protein or other additives such as bovine serum albumin BSA , human serum albumin HSA and sucrose, and lyophilized from low salt solution, so it often does not form a white grid structure, but a trace amount of protein deposit within the tube, forming a thin transparent or invisible protein layer.
Before opening the lid, we recommend to centrifuge in a small centrifuge for seconds firstly to ensure that the contents are on the bottom of the tube. Apart from a few exceptions, most human cytokines are active on mouse cells. Many mouse cytokines may also have effect on human cells, however, the activity may be lower than the corresponding human cytokines. One of the few human cytokines will be more active than corresponding mouse cytokines when acting on mouse cells, such as IL In contrast, fibroblast growth factor FGF and neurotrophin are highly conserved and both have good activity on cells of different species.
Commonly used preservative include Proclin , Sodium azide, etc. We do not add any preservative to our proteins.
What kind of protectant do you usually add? Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization. Protein expression is the biotechnological process of generating a specific protein.
It can be done in prokaryotic, eukaryotic or In vitro E. Protein purification is a series of processes intended to isolate one or a few proteins from cells or organisms. The most popular method for protein purification is affinity chromatography, and which is designed by different protein tags. Other protein purification methods, including ion exchange chromatography, size-exclusion chromatography, polish purification and hydrophobic interaction chromatography are available to handle tag-free proteins with high purity.
Incorrect vector construction.
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You should confirm vector by sequencing or apply for our custom clone service. Rare codons. You should optimize codons, use strains supplementing rare codons, induce at lower temperature or grow in poor media. Protein toxicity. You should use promoters with tighter regulation or lower plasmid copy number. Start induction at high OD and shorten induction time. Add glucose when using expression vectors containing lac-based promoters.
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Proteins with high hydrophobicity or transmembrane domains. You should add fusion tags or add heat shock chaperones. You should induce for a shorter time at low temperature or change to poor media. Generate truncated forms of protein or use membrane rich strains. Incorrect disulfide bond formation. You should add fusion partners, including thioredoxin, DsbA, DsbC. Clone in a vector containing secretion signal peptide to cell periplasm.
Use gamiB DE3 strains with oxidative cytoplasmic environment. Lower inducer concentration and induction temperature. Incorrect folding. You should use a fusion partner. Co-express with molecular chaperones. Use strains with cold-adapted chaperones. Supplement media with chemical chaperones and cofactors. Reduce the inducer concentration and add fresh media.
Induce for a shorter time at low temperature. Rare amino acids selenocysteine Sec or pyrrolysine Pyl in protein sequence. You should use some other amino acids to instead these two unusual amino acids. Imbalanced translation process of fusion protein. You should change another fusion tag or move fusion tag to C-terminal. Protein degradation. You should replace specific protease sites.
Use protease deficient strains. Induce at high OD. You should induce for a shorter time at low temperature or use protease inhibitors when breaking cells. Post-translational modification. Phosphorylation, glycosylation, etc which increases the size of the protein.
Post-translational cleavage. Many proteins are synthesized as pro-proteins, and then cleaved to give the active form. Relative charge. The composition of amino acids have different relative charge which will affect the electrophoretic mobility.
Multimers such as dimerisation of a protein. This is usually prevented in reducing conditions, although strong interactions can result in the appearance of higher bands. Protein structure such as disulfide bond, protein secondary structure or protein 3D structure formation. Hydrophobic proteins, such as transmembrane proteins, may have difficulties in migrating into the gel, and thus resulting in different multi-banded patterns.
For gaining a protein with bioactivity, you should choose a right expression system, a suitable expression vector , an appropriate purification method and a validation experiment. Otherwise, you can check the problems below:. Low solubility of the protein. You should fuse desired protein to a fusion partners and lower temperature. Lack of essential post translational modification. You should change another expression system. If Apple Books doesn't open, click the Books app in your Dock. Do you already have iTunes? Click I Have iTunes to open it now.
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