Protein L Recombinant Protein His Tag Lyophilized from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in 0.1 M NaH2PO4, pH8.5 with a purity of >98% as determined by SDS-PAGE..

More Details:

• Species: Bacteria-Derived
• Target:
• Purity: >98% as determined by SDS-PAGE.
• Source: E. coli
• Storage Conditions: Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles.

Additional Information:

Protein L was isolated from the surface of bacterial species Peptostreptococcus magnus and was found to bind Ig(IgG,IgM,IgA,IgE and IgD) through L chain interaction, from which the name was suggested. Despite this wide-ranging binding capability with respect to Ig classes, Protein L is not a universal immunoglobilin-binding protein. Binding of Protein L to immunoglobulins is restricted to those containing kappa light chains (i.e., k chain of the VL domain). In humans and mice, kappa (k) light chains predominate. The remaining immunoglobulins have lambda (l) light chains. The recombinant protein contains four immunoglobulin (Ig) binding domains (Bdomains) of the native protein. Besides antibody, protein L is also suitable for binding of a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs).

This recombinant protein can be used for WB. For research use only.. At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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