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Cat. No.: RPL-10 (for 10mg)

Cat. No.: RPL-100 (for 100mg)

Cat. No.: RPL-1k (for 1g)

Description

Recombinant Protein L contains 5 kappa-binding domains. Protein L was first isolated from the surface of bacterial species Peptostreptoccus magnus [1]. Unlike Protein A and Protein G, which bind to the Fc region of immunoglobulins (antibodies), Protein L binds antibodies through kappa light chain interactions without interfering with an antibody’s antigen-binding site. This gives Protein L the ability to bind a wider range of Ig classes and subclasses (IgG, IgM, IgA, IgE and IgD) than Protein A or Protein G. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L. Protein L binds kappa I, III, and IV in human and kappa I in mouse.

Purity    

>98% by SDS-PAGE and SEC-HPLC analyses.

Biological Activity    

The recombinant Protein L is a genetically engineered protein containing 5 IgG-binding regions of protein L. Cell wall binding region, cell membrane binding region and albumin binding region have been removed from the recombinant Protein L to ensure the maximum specific IgG binding. The recombinant Protein L is ideal for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to human, mouse, rat and pig IgG.

Physical Appearance    

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation    

Lyophilized from additive-free solution.

Endotoxin    

Less than 0.1EU/μg of Protein L as determined by LAL method.

Reconstitution    

Dissolve in distilled water or saline.
 

Amino Acid Sequence    

KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG

Only for research and not intended for treatment of humans or animals

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