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Lamarck Protein

I. Full-Range Protein Portfolio: Precisely Adapting to Diverse Research Needs

 

Based on the characteristic requirements of proteins in different research scenarios, Lamarck has created a differentiated product matrix that covers the entire demand chain from "basic mechanism exploration" to "applied technology development".

 

(I) Recombinant Proteins: Core Choice for Research and Applications

 

As the core of the product portfolio, Lamarck's recombinant proteins are produced using multiple expression systems (prokaryotic, eukaryotic, insect cell), enabling precise regulation of protein modification status and activity to meet different research objectives:

 

Eukaryotic-expressed recombinant proteins: Utilizing eukaryotic systems such as HEK293 and CHO cells, they can achieve natural post-translational modifications of proteins (e.g., glycosylation, phosphorylation). Their structure and activity are more similar to endogenous proteins, making them suitable for antibody development (as immunogens), cell function experiments (e.g., signal pathway activation research), and drug target validation.

 

Insect cell-expressed recombinant proteins: Combining the high efficiency of prokaryotic expression and the modification advantages of eukaryotic expression, they are suitable for proteins requiring complex folding or multi-subunit assembly (e.g., membrane proteins, viral antigens), providing high-quality antigens for virology research and vaccine development.

 

Prokaryotic-expressed recombinant proteins: Using E. coli as the expression host, they are suitable for proteins with simple structures that do not require complex post-translational modifications (e.g., enzymes, core domains of cytokines). They offer the advantages of high expression yield, low cost, and short production cycle, making them suitable for basic biochemical experiments (e.g., enzyme activity determination, preliminary screening of protein-protein interactions).

 

(II) Native Proteins: Research Tools for Restoring Physiological States

 

To meet the research demand of "retaining the natural structure and complex interactions of proteins", Lamarck has launched native protein products. These proteins are isolated from animal tissues and cells through gentle extraction and purification processes:

 

Gentle technologies such as hypotonic lysis and affinity chromatography are used during extraction to avoid protein denaturation and fully retain their natural conformation and biological activity.

 

The product range includes serum proteins (e.g., human serum albumin, HSA) and tissue-specific proteins (e.g., liver-derived metabolic enzymes). They are suitable for research such as "in vivo functional simulation of proteins" and "structural analysis of natural complexes", providing a basis for exploring the real role of proteins in physiological environments.

 

(III) Protein Standards: "Benchmark" for Experimental Quantitation and Quality Control

 

To ensure the accuracy and reproducibility of experimental results, Lamarck provides high-purity protein standards, which are mainly divided into two functional categories to precisely meet the quality control needs of different experimental scenarios:

 

Quantitative Standards: Serving as the "reference benchmark" for protein concentration determination, they cover two subcategories: classic universal standards and target-specific standards. Among them, BSA (bovine serum albumin) standards are the first choice for routine laboratory protein quantitation experiments (e.g., BCA assay, Bradford assay, Lowry assay). Their amino acid composition is similar to that of most eukaryotic proteins, which can effectively reduce determination deviations. Recombinant cytokine standards with known concentrations (e.g., recombinant human IL-6, TNF-α standards) are designed for specific target protein quantitation scenarios (e.g., enzyme-linked immunosorbent assay, ELISA; Western Blot semi-quantitative analysis). With pre-set precise concentrations (usually labeled in ng/mL or pg/mL), they help generate standard curves with high linearity, enabling direct and accurate calculation of target protein concentrations in samples and avoiding quantitation errors caused by differences in protein properties.

 

II. Rigorous Quality Control System: Ensuring Product Performance with "Three High Standards"

 

Throughout the entire process from expression, purification to packaging of Lamarck's protein products, a quality control system higher than industry standards has been established to ensure that each batch of products meets the requirements of "high purity, high activity, and high stability".

 

(I) High Purity: Eliminating Impurity Interference

 

Purity is detected by methods such as SDS-PAGE electrophoresis and high-performance liquid chromatography (HPLC). The purity of recombinant proteins is generally ≥95%, and core products (e.g., antigen proteins for antibody development) can reach a purity of over 98%.

Endotoxin content is strictly controlled (detected by LAL chromogenic assay). The endotoxin content of eukaryotic-expressed recombinant proteins is ≤1 EU/μg, meeting the low-toxicity requirements of cell experiments and animal experiments, and avoiding endotoxin interference with cell activity and experimental results.

 

(II) High Activity: Restoring Physiological Functions

 

Exclusive activity detection protocols are designed for different protein types: For enzyme proteins, enzyme activity is determined through substrate catalytic reactions (e.g., colorimetry, fluorimetry); for cytokines, activity is verified by their ability to regulate the proliferation/apoptosis of target cells (e.g., MTT assay, flow cytometry); for receptor proteins, binding activity is detected through ligand-binding experiments (e.g., ELISA, SPR).

Activity detection results are benchmarked against native proteins or international standards to ensure that the biological functions of recombinant proteins are consistent with endogenous proteins, thus guaranteeing the reliability of experimental results.

 

(III) High Stability: Adapting to Experimental Scenarios

 

Protein storage buffer formulations are optimized (e.g., adding glycerol, protease inhibitors, stabilizers). Two forms (lyophilized powder and liquid) are provided based on protein characteristics: Lyophilized powder can be stored long-term at -20℃; the liquid form is convenient for immediate use and avoids protein denaturation caused by repeated freeze-thaw cycles.

Product stability is verified through accelerated stability tests (e.g., storage at 37℃ for 7 days, repeated freeze-thaw at -20℃ for 5 cycles) to ensure that proteins maintain their activity and purity during transportation, storage, and experimental processes.

 

III. Core Application Scenarios: Penetrating the Whole Field of Life Sciences Research

 

With excellent performance, Lamarck's protein products are widely used in key links of basic research and application development:

 

Basic mechanism research: For example, recombinant cytokines are used in the study of signal pathway (e.g., JAK-STAT, NF-κB) activation mechanisms; native proteins are used in the exploration of protein-protein interactions (e.g., Co-IP, Pull-down).

 

Antibody and diagnostic reagent development: High-purity recombinant proteins are used as immunogens for the preparation of monoclonal and polyclonal antibodies; protein standards are used for the calibration and quality control of diagnostic kits (e.g., ELISA kits).

 

Drug development: Recombinant receptor proteins are used for drug target screening (e.g., detection of binding affinity between small-molecule drugs and receptors); native enzyme proteins are used for the activity evaluation of enzyme inhibitor drugs.

 

Cell and animal experiments: Low-endotoxin recombinant proteins are used in cell culture (e.g., stem cell differentiation induction) and animal model construction (e.g., cytokine intervention experiments in inflammation models).


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