Name: Recombinant Protein Expression Service
Brand: Tsingke Biotech
SKU: 00305
Availability: InStock
Rating: 5 (1 reviews)

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Home » Product & Services » Protein Expression » Recombinant Protein Expression Service

Overview

In response to the growing need for swift and high-throughput protein and antibody research, Tsingke introduced our pioneering Recombinant Protein Expression Service. Tailored to meet the dynamic requirements of the evolving research landscape, particularly amid the rapid advancements in antibody drug development, this service ensures rapid delivery by leveraging a high-throughput transient transfection expression platform.

Tsingke offers a comprehensive one-stop service, that covers gene synthesis, protein structure analysis and design, protein expression, as well as efficient transfection and purification. Committed to guiding researchers at every step, our Recombinant Protein Expression Service aims to maximize the success of research projects, accelerating the journey toward groundbreaking discoveries.

Advantages

Versatile Options

Tailor expression with diverse choices in promoters, vectors, hosts, and fusion tags

High expression level

Utilizing codon optimization along with QC and protein purity, activity, and endotoxin levels testing

High success rate

Successfully expressed over a hundred proteins in mammalian system

Service Details

Service Name	Service Code	Service Details	Turnaround Time
Escherichia Coli Expression System	Tsingke-001	Codon Optimization and Gene Synthesis	1~2 weeks
		Subcloning	1~2 weeks
		Expression testing and purification (optimized under various conditions)	2~3 weeks
		Shipment of samples	-
		Experiment report	-
Bacillus Subtilis Expression System	Tsingke-002	Codon Optimization and Gene Synthesis	1~2 weeks
		Subcloning	1~2 weeks
		Expression purification testing	2~3 weeks
		1 L fermentation purification	1~2 weeks
		Shipment of samples	-
		Experiment report	-
Yeast Expression System	Tsingke-003	Codon Optimization and Gene Synthesis	1~2 weeks
		Subcloning	1~2 weeks
		Antibiotic screening	1 week
		Pilot protein expression evaluation (2 positive clones will be used to verify the expression, conducting optimization of methanol concentration and induction time.)	1~2 weeks
		Purification testing (using the optimal clone under the best expression conditions for a 100 mL expression purification)	1~2 weeks
		1 L fermentation purification	1~2 weeks
		Shipment of samples	-
		Experiment report	-
Insect Expression System	Tsingke-004	Codon Optimization and Gene Synthesis	1~2 weeks
		Subcloning	1~2 weeks
		P1 virus stock generation and expression testing (Plasmid transformation, bacterial growth, blue-white screening, plasmid extraction, transfection, P1 expression verification, SDS-PAGE or Western blot)	2~3 weeks
		P2 virus stock generation and optimization of expression conditions (P2 virus generation, MOI testing, SDS-PAGE or Western blot)	2~3 weeks
		200 mL expression purification testing and protein sample delivery	1 week
		1 L insect cell scale expression and purification	1~2 weeks
		Shipment of samples	-
		Experiment report	-
Mammalian Expression System	Tsingke-005	Codon Optimization and Gene Synthesis	1~2 weeks
		Subcloning	1~2 weeks
		80 mL expression testing	1~2 weeks
		1 L scale expression and purification	1~2 weeks
		Shipment of samples	-
		Experiment report	-

Deliverables

Delivery Standard

Purified protein; QC analysis.

Optional：

Plasmid contain gene of interest; HPLC-SEC; Endotoxin test; MS etc.

Evaluate each order’s SDS-PAGE result

Workflow

Case

Picture 1: Protein expression in Mammalian Cell

Picture 2: ProteinX expression in Escherichia Coli

Related Resource

Tsingke_Recombinant Antibody Flyer-V1.1.1.240129

FAQ

Can membrane proteins be expressed in full length?

Transmembrane proteins have highly hydrophobic transmembrane regions, making full-length expression very challenging (see Why are transmembrane proteins difficult to express?). Even if expression is successful, the yield is typically low because the cell membrane area is limited and cannot support the attachment of large amounts of membrane proteins. Additionally, the final purification yield is also usually low.

Generally, membrane proteins function primarily through their extracellular or intracellular domains. If full-length expression is not strictly necessary, it is recommended to focus on expressing these specific domains. However, if full-length expression is still required, it is advisable to consider using a cell-free expression system for testing.

How are charges handled for expression failures?

Failure criteria: Delivery is based on the presence of the target band in SDS-PAGE detection. For potential protein degradation, since degradation is related to the protein's inherent properties and cannot be completely avoided by the expression system, efforts will be made to optimize the process during the experiment, but we cannot guarantee the absence of degradation.

Regarding inclusion bodies, since inclusion bodies are a form of the protein present in the body, inclusion bodies also meet the delivery standard. However, this is only applicable if the client can accept the renaturation of inclusion body proteins.

If the above conditions are not met, the project will be considered a failure. In such cases, we will share half of the expression testing costs with the client. The client will only need to pay the full cost of gene synthesis, full cost of vector construction, and 50% of the expression testing cost, with the remaining 50% of the expression testing cost covered by the company.

How long can proteins typically be stored?

Proteins can generally be stored at -80°C for 1-3 months, and at 4°C for 1-2 weeks. For proteins with poor stability outside the body, the storage time may be shorter, and this should be assessed based on the specific protein. It is recommended to aliquot the protein into appropriate portions (preferably in amounts for each use), store it at -80°C, and avoid repeated freeze-thaw cycles.

Is functional activity verification of proteins possible?

Since the functional activity testing standards for each protein vary, it involves the development of detection methodologies. This may also include the development of protein-related receptors or the detection of other proteins in the cell pathway. It is recommended that you design the testing and verification according to your specific experimental needs in the later stages.

What is the typical timeline for the protein expression process?

The typical timeline is as follows:

Gene synthesis: 1-2 weeks

Vector construction: 1 week

Expression testing:

Prokaryotic (E. coli): 1 week

Eukaryotic: 1-2 weeks

Scale-up production:

Prokaryotic (E. coli): 1-2 weeks

Eukaryotic: 2-3 weeks

The total timeline is:

Prokaryotic (E. coli): 3-5 weeks

Eukaryotic (mammalian cells): 4-5 weeks

How much protein can be delivered at the end, and what is the purity?

For the E. coli protein expression system, we charge based on the quantity. The standard small-scale trial delivers 1 mg of protein with 85% purity. If larger quantities are required, such as 100 mg, 1 g, 10 g, or 100 g, a small-scale expression test is first conducted, followed by a scaling evaluation and quote.

For mammalian, Bacillus, yeast, insect, and other expression systems, we generally calculate based on the expression volume. Since the characteristics of each protein are different, protein expression levels can vary under the same expression volume, ranging from 50 µg to several milligrams. We will deliver all the expressed and purified protein, with purity typically greater than 85%. If a higher purity is required, we can perform secondary purification to enhance the purity (which may incur additional costs).

What is the role of lyophilization protectants?

Protectants are used to safeguard proteins during freeze-drying and storage. Common protectants or stabilizers include sugars, polyols, polymers, surfactants, certain proteins, and amino acids. Among these, trehalose and mannitol are commonly used.

Trehalose can significantly prevent changes in the secondary structure of proteins and inhibit protein unfolding and aggregation during the freeze-drying process. Mannitol is also a widely used freeze-drying protectant and filler, which can reduce aggregation of certain proteins after freeze-drying.

Why is lyophilization required for proteins? What impact does lyophilization have on proteins?

Proteins are heat-sensitive, and freeze-drying can preserve the activity of most proteins, improving their stability and extending their shelf life, while also reducing shipping costs.

However, freeze-drying may cause partial loss of protein activity, aggregation, and other denaturation issues. These negative effects can be minimized by adding protectants (such as stabilizers, additives, and excipients) and carefully controlling various freeze-drying conditions.

How is a protein purified? Is its purity guaranteed?

Design the optimal purification scheme based on the type of fusion protein tag and the physicochemical properties of the protein itself. Common purification methods include affinity chromatography, hydrophobic interaction chromatography, ion exchange chromatography, and size exclusion chromatography, among others. Our guaranteed minimum purity standard is greater than 85%. If the initial purification does not meet this standard or if the customer has higher purity requirements, we also have the AKATA purification system. This system is highly automated, with precise control, and when combined with various columns, ensures that the purity of our protein products is further improved. The final purity test results will be displayed in the COA report.

**For Research Use Only. Not for use in diagnostic procedures.

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Tsynth™ Gene Synthesis

Standard Gene Synthesis

ProLongGene

DNA Fragment

ssDNA

PCR Cloning & Subcloning

Site-directed Mutagenesis

Plasmid Preparation

Protein Expression

Recombinant Protein Expression Service

Oligo Synthesis

Antibody Service

Recombinant Antibody Expression

Application

Small Nucleic Acid Drug

In Vitro Diagnostic (IVD)

Synthetic Biology Solutions

Gene Regulation

Virus Packaging

Cell Line Construction

Library Construction