POP4 Human
Description
POP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Introduction
The processing of precursor 4 (human recombinant) involves a series of biochemical and biotechnological steps to produce a functional protein from its precursor form. This process is crucial in the field of recombinant protein production, which has significant applications in medicine, research, and biotechnology.
Recombinant Protein Production
Recombinant protein production involves the insertion of a gene encoding the desired protein into a host organism, such as bacteria, yeast, or mammalian cells. The host organism then expresses the protein, which can be harvested and purified for various applications. The precursor 4 protein is initially produced in an inactive form and requires specific processing steps to become active.
Processing Steps
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Gene Cloning and Expression: The gene encoding precursor 4 is cloned into an expression vector, which is then introduced into a suitable host organism. The host cells are cultured under conditions that promote the expression of the recombinant protein.
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Protein Extraction: Once the host cells have produced the precursor protein, it is extracted from the cells. This typically involves cell lysis, where the cells are broken open to release their contents, including the recombinant protein.
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Purification: The extracted protein is then purified using various chromatographic techniques. This step is crucial to remove impurities and obtain a high-purity protein product. Common methods include affinity chromatography, ion exchange chromatography, and size exclusion chromatography.
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Folding and Refolding: Recombinant proteins often require proper folding to achieve their functional conformation. This step may involve the use of chaperones or specific conditions that promote correct folding. In some cases, the protein may need to be refolded if it was initially produced in an incorrect conformation.
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Post-Translational Modifications: Some recombinant proteins require post-translational modifications, such as glycosylation or phosphorylation, to become fully functional. These modifications are typically carried out by the host cells or through additional enzymatic steps.
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Activation: The precursor 4 protein is initially produced in an inactive form and requires specific processing steps to become active. This may involve proteolytic cleavage, where specific enzymes cleave the precursor protein at defined sites to generate the active form.
Applications
The processed precursor 4 (human recombinant) protein has various applications in research and medicine. It can be used as a therapeutic agent, a diagnostic tool, or a research reagent. The ability to produce recombinant proteins in large quantities has revolutionized the field of biotechnology and has led to the development of numerous life-saving therapies.
Conclusion
The processing of precursor 4 (human recombinant) is a complex and multi-step process that involves gene cloning, protein expression, extraction, purification, folding, post-translational modifications, and activation. Each step is crucial to ensure the production of a high-quality and functional protein product. The advancements in recombinant protein production have opened up new possibilities in medicine and research, making it an essential area of study in biotechnology.
