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I-5™ 2X Hi-Fi PCR Master Mix
I-5 High-Fidelity DNA Polymerase is an ultra-high fidelity and high processivity enzyme. It produces the most accurate copies of DNA, and performs at an ultra-high rate. I-5 is perfect for applications such as cloning amplified material for protein expression in vitro, SNP analysis by sequencing, and high-specificity PCR.

Please note: 2X Hi-Fi HTP PCR Master Mix has been replaced with I-5™ 2X Hi-Fi PCR Master Mix for enhanced fidelity.

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I-5™ Hi-Fi DNA Polymerase

I-5 Hi-Fi DNA polymerase is an ultra-fast and high-fidelity DNA polymerase. It provides robust amplification from different templates including plasmids, BACS, genomic DNA, and lambda DNA.

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I-5™ Hi-Fi HotStart DNA Polymerase

I-5 Hi-Fi DNA HotStart Polymerase is a high-fidelity and fast DNA polymerase.

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IDA Agarose for His-tagged Recombinant Proteins  (C.)
Ni2+, Co2+, Cu2+, or Zn2+ charged nitrilotriacetic acid (NTA) coupled to Agarose CL-6B via a stable and uncharged long ether hydrophilic spacer arm, and offers high binding capacity and minimal non-specific binding.

Also Available FastSep™ High Performance IDA Resins
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IDA Agarose for His-tagged Recombinant Proteins  (R.)
Ni2+, Co2+, Cu2+, or Zn2+ charged iminodiacetic acid (IDA) coupled to Agarose CL-6B via a stable and uncharged long ether hydrophilic spacer arm, and offers high binding capacity and minimal non-specific binding.

Also Available FastSep™ High Performance IDA Cartridges
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IgG Purification using Protein A
Recombinant Protein A is an immunoglobulin-binding protein derived from the cell wall of the bacterium Staphylococcus aureus. It is composed of five homologous Ig-binding domains that fold into a three-helix bundle. Each domain is able to bind proteins from many of mammalian species, most notably IgGs. Protein A binds with high affinity to human IgG1 and IgG2 as well as mouse IgG2a and IgG2b. Protein A binds with moderate affinity to human IgM, IgA and IgE as well as to mouse IgG3 and IgG1. It does not react with human IgG3 or IgD, nor will it react to mouse IgM, IgA or IgE.
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IgG purification using Protein G
Recombinant Protein G is an immunoglobulin-binding protein derived from the cell wall of certain strains of b-hemolytic Streptococci. It binds with high affinity to the Fc portion of various classes and subclasses of immunoglobulins from a variety of species. The albumin and cell surface binding domains have been eliminated from Recombinant Protein G to reduce nonspecific binding and, therefore, can be used to separate IgG from crude samples. Due to its affinity for the Fc region of many mammalian immunoglobulins, protein G is a major application in purifying antibodies. Protein G is considered a universal reagent in biochemistry and immunology.
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Inorganic Pyrophosphatase, <i>E. coli</i>
Inorganic pyrophosphatase (PPase) is ubiquitous in nature and plays an important role in energy metabolism, providing a thermodynamic pull for biosynthetic reactions such as protein, RNA, and DNA synthesis.
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Inorganic Pyrophosphatase, Thermostable
A modified Enzyme, catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate.
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Inorganic Pyrophosphatase, yeast
The Pyrophosphatase, inorganic (PPase) catalyzes the hydrolysis of inorganic pyrophosphate to two orthophosphates
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IPTG, 1 M

IPTG (isopropyl-beta-D-thiogalactopyranoside) is a highly stable synthetic analog of lactose. It inactivates the lac repressor and induces synthesis of beta-galactosidase, an enzyme that promotes lactose utilization. IPTG is used to induce expression of cloned genes under the control of the lac operon (1).

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