Cat. No: AX-AP01012A Size: 100 ug
Protein L, cl-APC conjugated
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. The recombinant protein contains four immunoglobulin (Ig) binding domains (Bdomains) of the native protein. Recombinant Protein L Protein, fused with the polyhistidine tag at N-terminus and a single cysteine at C-terminus. DTT-reduced protein migrates as a 36 to 38 kDa polypeptide.
Allophycocyanin (APC), purified from Spirulina, is made up of alpha and beta subunits and is present as a trimer (αβ)3, which is unstable and susceptible to dissociation at low concentrations. The monomer, αβ, has a lower fluorescence quantum yield compared to the trimer and the maximal absorption is also shifted to 620 nm. The chemically cross-linked APC trimer (cl-APC) is much more stable than the native APC trimer, but still retains the same spectroscopic properties as the native APC trimer.
Protein L, cl-APC conjugated is a protein labeled by cl-APC.
Formulation: 100 µg of Protein L conjugated with cl-APC in PBS.
Excitation Laser: Red Laser (651 nm)
Application: In 0.1 ml PBS
Immunofluorescence (IF) 1: 50-1:200
Flow cytometry 1: 100-1:500.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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). 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.
This product is for research use only. It is not approved for use in humans, animals, or in vitro diagnostic procdures.
There are no reviews yet.