Biotinylated Recombinant Protein L, His, Avitag™ (MALS & FACS verified)

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 protein carries a polyhistidine tag at the N-terminus, followed by an Avi tag (Avitag™) . The protein has a calculated MW of 43.7 kDa. The protein migrates as 50 kDa under reducing (R) condition (SDS-PAGE) .

-20°C to -70°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Immobilized Mouse Human chimeric Anti-BCMA mAb (Aa01, Mouse IgG1) at 2 μg/mL (100 μL/well) can bind Biotinylated Recombinant Protein L, His,Avitag (Cat. No. RPL-P81Q7) with a linear range of 0.2-2 ng/mL (QC tested).