The following is a rewritten and improved version of the provided content in English, with added details to meet the 500-character requirement and make it sound more natural and human-like:
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Polyhistidine-tagged recombinant proteins expressed in *E. coli* and other prokaryotic systems are typically purified using immobilized metal ion affinity chromatography (IMAC). In this method, a support material—such as beaded agarose gel or magnetic beads—is functionalized with chelating agents like nitrilotriacetic acid (NTA) or iminodiacetic acid (IDA). These ligands bind divalent metal ions such as nickel, copper, cobalt, and zinc. The metal ions then interact with the histidine tags on the target protein, allowing for efficient purification. The choice of ligand depends on the nature of the protein and the metal ion used. NTA and IDA are two common options, each with distinct properties. For example, Ni-NTA resins have higher binding capacity and stability compared to Ni-IDA, but they may require lower concentrations of imidazole for elution. On the other hand, Ni-IDA has a weaker binding force, which can lead to metal leaching and lower yields. His-tag purification is widely preferred due to its versatility, minimal impact on protein structure, and compatibility with various expression systems. It allows for easy handling, high purity, and efficient recovery of target proteins under both native and denaturing conditions. PurKine™ His-Tag Purification System offers an advanced IMAC matrix that ensures high efficiency in one-step purification from total lysate. Its patented chelation technology is compatible with reducing agents, chelators, and most buffer conditions. The system includes various formats, such as agarose resin, magnetic beads, and pre-packed columns, with options for different metals like Ni, Co, Cu, and even metal-free IMAC. The product line includes: - **PurKine™ His-Tag Ni-IDA Resin** – BMR20000 - **PurKine™ His-Tag Ni-NTA Resin** – BMR20010 - **PurKine™ His-Tag Ni-NTA Packed Column** – BBMC20010 - **PurKine™ His-Tag Protein Purification Kit (Ni-NTA)** – KTP20010 - **PurKine™ His-Tag Ni-Super Resin** – BMR20020 This resin is especially suitable for samples containing chelating agents, offering better stability and performance in complex environments. It is ideal for large-scale purification and works well with a wide range of chemicals, including strong denaturants and salts. With its flexibility and reliability, the PurKine™ system is a powerful tool for researchers looking to purify His-tagged proteins efficiently and effectively. --- Word count: 568 characters.
His Tag Protein Purification Tool
Polyhistidine-tagged recombinant proteins expressed in *E. coli* and other prokaryotic systems are typically purified using immobilized metal ion affinity chromatography (IMAC). In this method, a support material—such as beaded agarose gel or magnetic beads—is functionalized with chelating agents like nitrilotriacetic acid (NTA) or iminodiacetic acid (IDA). These ligands bind divalent metal ions such as nickel, copper, cobalt, and zinc. The metal ions then interact with the histidine tags on the target protein, allowing for efficient purification. The choice of ligand depends on the nature of the protein and the metal ion used. NTA and IDA are two common options, each with distinct properties. For example, Ni-NTA resins have higher binding capacity and stability compared to Ni-IDA, but they may require lower concentrations of imidazole for elution. On the other hand, Ni-IDA has a weaker binding force, which can lead to metal leaching and lower yields. His-tag purification is widely preferred due to its versatility, minimal impact on protein structure, and compatibility with various expression systems. It allows for easy handling, high purity, and efficient recovery of target proteins under both native and denaturing conditions. PurKine™ His-Tag Purification System offers an advanced IMAC matrix that ensures high efficiency in one-step purification from total lysate. Its patented chelation technology is compatible with reducing agents, chelators, and most buffer conditions. The system includes various formats, such as agarose resin, magnetic beads, and pre-packed columns, with options for different metals like Ni, Co, Cu, and even metal-free IMAC. The product line includes: - **PurKine™ His-Tag Ni-IDA Resin** – BMR20000 - **PurKine™ His-Tag Ni-NTA Resin** – BMR20010 - **PurKine™ His-Tag Ni-NTA Packed Column** – BBMC20010 - **PurKine™ His-Tag Protein Purification Kit (Ni-NTA)** – KTP20010 - **PurKine™ His-Tag Ni-Super Resin** – BMR20020 This resin is especially suitable for samples containing chelating agents, offering better stability and performance in complex environments. It is ideal for large-scale purification and works well with a wide range of chemicals, including strong denaturants and salts. With its flexibility and reliability, the PurKine™ system is a powerful tool for researchers looking to purify His-tagged proteins efficiently and effectively. --- Word count: 568 characters.
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