FITC-Labeled Recombinant Protein L, His Tag (Cat. No. RPL-PF141) is expressed from human HEK293 cells. It is the FITC labeled form of Recombinant Protein L (Cat. No. RPL-P3141).
FITC-Labeled Recombinant Protein L, His Tag is fused with a polyhistidine tag at the N-terminus. The reducing (R) protein migrates as 40-45 kDa in SDS-PAGE.
Excitation source: 488 nm spectral line, argon-ion laser
Excitation Wavelength: 488 nm
Emission Wavelength: 535 nm
The primary amines in the side chains of lysine residues and the N-terminus of the protein are conjugated with FITC using standard chemical labeling method. The residual FITC is removed by molecular seive treatment during purification process.
The FITC to protein molar ratio is 5-7.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please protect from light and avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
FITC-Labeled Recombinant Protein L, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Immobilized Yervoy Ipilumimab at 10 μg/mL (100 μL/well) can bind FITC-Labeled Recombinant Protein L, His Tag (Cat. No. RPL-PF141) with a linear range of 20-156 ng/mL (Ex.488 nm/Em.535 nm) (QC tested).
CAR阳性表达率检测（Evaluation of CAR expression ）
FACS Analysis of anti-CD19 CAR Expression
293 cells were transfected with anti-CD19-scFv and RFP tag. 2e5 of the cells were stained with FITC-Labeled Recombinant Protein L, His Tag (Cat. No. RPL -PF141, 10 µg/ml). FITC Streptavidin was used as negative control.
Authors: Bruniaux J, et al
Journal: Int J Pharm 2019
Application: Microscopic imaging
Authors: Luo M, et al
Journal: Appl Microbiol Biotechnol 43542
Application: Flow cytometry
Authors: TW Chang, et al.
Journal: US20180264133A1 43363
Authors: Jiasen Xie, et al.
Journal: Oncol Lett 2018
Authors: Hervé-Aubert K, et al.
Journal: Bioconjug Chem 2018
Authors: Alric C, et al.
Journal: J Nanobiotechnology 2018
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).