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Endo-Remover, a superior Adsorbent for Removal of Endotoxin from Biomolecular Solutions | 生物样品脱内毒5分钟搞定

产品编号:P101

包装:100mg, 250mg, 500mg, 1g

价格:180, 329, 589,999

Endo-Remover Adsorbent

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A Superior Adsorbent Developed at pae for Removal of Endotoxin from Biomolecular Solutionsm
生物样品脱内毒5分钟搞定
 

Features:

  • Very effective removal of endotoxin, up to 99.99% of the original endotoxin removed
  • Simple and fast,  only mix and spin or filtration, 5 mins finished
  • Very high binding affinity  to endotoxins , up to 10^-10 M^-1
  • Nanoparticle with extreamly large area providing very High binding capacity to endotoxins, adsorbe up to 3.9 × 10^4 EU per mg adsorbent
  • Very high binding specificity to endotoxins and low binding to most proteins and nucleic acids, resulting protein recovery over 80% on average.
  • Endotoxin binding is entially independent of pH, conductivity, reducing agent and various organic solvents, and compatible with almost all biomaterial solutions containning proteins, nucleic acids, etc
  • DNA samples prepared with this reagent is suitalbe for transfection in vivo or in vitro
  • Economic: pae provide affordable price for small and large scale application
  • Effective from low (<10 EU/mL) to very high (>10^6 EU/mL) endotoxin concentrations
This product is independent on NaCl concentration up to 0.5M, pH from 3 to 9.5. It is compatable with many solutions, such as HEPES, Tris,etc. But, formamide, urea, and diazolidinyl urea at high concentration inhibite the binding of this product to endotoxin. 
Cat No CAS No. NAME/ Chinese Name Storage Purity/Grade   Package/Your Price
P101 N/A Endo-Remover | 内毒素清除剂  2-8℃ ≥98% BioReagent 100 mg 180 250 mg 329 500mg 589 1g  999

 

Other Names: 液相内毒素清除剂, 固相内毒素清除剂,  pyrogen, LPS
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Since the discovery of endotoxins (also called as pyrogen, LPS, etc) as the primary toxic component of Gram-negative bacteria, researchers have pursued the quest for molecules that detect, neutralize, and remove endotoxins. Selective removal of endotoxins is particularly challenging for protein solutions and, to this day, a general method for removing endotoxins from protein solutions is lacking. Endotoxins are negatively charged lipopolysaccharides, and current methods for endotoxin removal from protein solutions mostly exploit ionic and/or hydrophobic interactions with endotoxin molecules. While effective for certain proteins, these methods have several limitations. Methods using ion-exchange adsorbents are sensitive to pH and salt concentration and are generally not suitable for acidic protein Methods using hydrophobic adsorbents are less effective and are sensitive to salts and organic modifiers like solvents and detergent. Biological affinity-based methods, which generally depend on a combination of ionic and hydrophobic interactions, may be robust over a wider range of conditions but generally impose high costs and risk of contamination by toxic affinity ligands. Other endotoxin removal methods such as ultrafiltration and detergent-based extraction are generally not suitable for protein solutions due to their limited effectiveness, difficulty to remove residual detergents, and negative effects on protein stability and activity.

Endotoxins are of great concern in biological preparations as they interfere with cell-based assays and render biological products unsafe for therapeutic use. Endotoxins, also called lipopolysaccharides, originate from the cell surface of Gram-negative bacteria. They are widely present in the environment and human exposure to low levels of endotoxins elicit strong immune responses which can lead to fever, endotoxic shock and even death. Contamination with endotoxins is therefore a common problem and effective methods for removing endotoxins are needed to obtain reliable biological preparations for therapeutic use.
Although several methods and materials have been developed to this end, meeting regulatory or assay-specific threshold levels of endotoxins can be challenging. Achieving low endotoxin levels is particularly challenging for proteins, and reduction of endotoxins below 10 endotoxin units (EU) per mg protein is considered one of the most difficult steps during purification of proteins expressed in Escherichia coli.

Methods Removing Endotoxins
Solid phase adsorbents for removing endotoxins from protein or nucleic acid solutions include anion-exchange, hydrophobic, biological affinity and mixed mode materials.
Anion-exchange materials can strongly bind the negatively charged core polysaccharide region and the lipid A part of endotoxins, but their performance depends on pH and salt concentration and their use is generally limited to neutral and basic proteins. Hydrophobic materials may bind the fatty acyl chains of the lipid A part of endotoxins, but they are generally less effective and their performance depends on the presence of kosmotropic salts and organic modifiers. Biological affinity and mixed-mode chromatographic materials combining hydrophobic and ionic interactions may be less sensitive to buffer conditions; yet, they generally impose higher costs and they may leak toxic ligands into the final product. Additional limitations of these materials may include limited compatibility with sanitizing agents, low product recoveries and time-consuming equilibration and regeneration steps.
Aqueous two-phase is another established method for removing endotoxins from biomaterial solutions. Micellar extraction with the nonionic detergent Triton X-114. Endotoxins preferentially partition to the hydrophobic detergent-rich phase, whereas proteins prefer the aqueous phase. This enables up to 99% endotoxin removal from biomaterial solutions. However, relatively high process costs, difficulty to remove residual detergent and negative effects on protein activity disfavor the use of Micellar extraction methods in protein purification processes.
Metal affinity is an alternative methods for removing endotoxins. Interactions of endotoxins with free metals enable selective precipitation of endotoxins from plasmid DNA. Various metal salts were tested and the best results were obtained with zinc sulfate, which removed more than 80% of endotoxins with about 90% plasmid recovery. The effectiveness of precipitation based techniques for removing endotoxins from protein solutions remains however to be shown. Solid phase adsorbents involving metal interactions include immobilized metal affinity chromatography (IMAC), hydroxyapatite and calcium silicate materials. IMAC purification of an antibody fragment of E. coli lysate provided only limited endotoxin removal with residual endotoxin levels >104 EU/mL. An additional oncolumn washing step with Triton X-114 improved endotoxin clearance by >3 logs. This suggests that endotoxin removal by metal affinity purification is only effective when combined with other interaction mechanisms such as hydrophobic interactions with detergents. Chromatographic purification by hydroxyapatite was able to remove >4 logs of endotoxins of a native IgG pool. Aside from metal affinity interactions, retention of solutes by hydroxyapatite involves ionic interactions. This explains why purification results by hydroxyapatite generally depend on protein isoelectric point and solution conditions including pH and salt concentration. Similarly, endotoxin binding by calcium silicate was found to be highly dependent on the presence of salts.
 
Ultrafiltration
 

Reference: omitted
 

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