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",
"Country": "XG",
"Code": "Content",
"Name": "Content"
},
{
"Language": "en",
"Value": "In contrast to other available resins, which are primarily based on NTA or IDA chelator chemistry, this resin tolerates buffers that contain EDTA. Because EDTA is a known inhibitor of metalloproteases - which are frequently present in any cell type - this chromatography material provides the option to protect your target protein by supplementing your buffers with EDTA.
This resin therefore allows the easy purification of your target protein, while using an effective protection against degradation. The His-Tag binding principle allows a standard one-step isolation procedure, generally for all low- and high-molecular weight proteins. Using a special strong-binding Ni2+ chelator, minimal contamination of your fractions with metal ions is ensured, safeguarding your downstream applications.
Application The most common technique in affinity purification of proteins involves engineering a sequence of 6 to 14 histidines into the N- or C-terminal (or even on an exposed loop) of the protein. Such polyhistidine stretches bind strongly to divalent metal ions such as nickel and cobalt. This effect can be used to separate proteins. Metal ions can be immobilized on a matrix using a chelator, which still allows the ion to interfere with the polyhistidine tag of the protein. When these his-tagged proteins are passed through a column containing immobilized metal ions, the proteins bind via the tag to the column. Nearly all untagged proteins pass through the column. The protein is released from the column by elution with either imidazole, which competes with the polyhistidine tag for binding to the column, or by a decrease in pH, which decreases the affinity of the tag for the resin. While this procedure is generally used for the purification of recombinant proteins with an engineered affinity tag, it can also be used for natural proteins with an inherent affinity for divalent cations. ",
"Country": "XG",
"Code": "Product Description",
"Name": "Product Description"
},
{
"Language": "en",
"Value": "cOmplete His-Tag Purification Resin is function tested using the following procedures:
Binding capacity is determined using the His-tagged T4 gene 32 protein under standard conditions.
Ni2+ leakage is tested by incubating the resin with buffer supplemented with 10 mM DTT, 10 mM EDTA, and 500 mM imidazole for 1 hour. The amount of Ni2+ in the supernatant is quantified by ICP-MS.
",
"Country": "XG",
"Code": "Quality Control",
"Name": "Quality Control"
},
{
"Language": "en",
"Value": "cOmplete His-Tag Purification Resin can be used for small or large-scale purification of His-tagged proteins in biopharma manufacturing, yielding highly purified proteins from crude lysates. This resin can be used for batch or column chromatography procedures, and allows for target protein purification using both native and denaturing conditions. cOmplete His-Tag Purification Resin is compatible with common reducing agents and chelators while preventing contamination of the protein preparation with heavy metals.",
"Country": "XG",
"Code": "Applications",
"Name": "Applications"
},
{
"Language": "en",
"Value": "Matrix: Sepharose-CL 6B Bead size: 45 to 165 μM Binding Capacity: ≥40 mg protein per mL Note: The binding capacity of the resin to varíous types of proteins may vary according to the protein characteristics such as the molecular size of the protein.",
"Country": "XG",
"Code": "Specification",
"Name": "Specification"
},
{
"Language": "en",
"Value": "cOmplete His-Tag Purification Resin is a sepharose-based, pre-charged, ready-to-use Ni2+ chelate resin for small and large-scale purification of His-tagged proteins. It allows for the production of highly pure proteins from crude lysates, using a one-step purification process.",
"Country": "XG",
"Code": "Properties",
"Name": "Properties"
},
{
"Language": "en",
"Value": "Will be supplied as \"cOmplete His-tag Purific. Resin 800ml\". Unit of measure is “piece”.",
"Country": "XG",
"Code": "CB - Order Information",
"Name": "CB - Order Information"
}
]
}
}
]
}
