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Safety Data Sheet (SDS) Purified Anti-Lck Antibody     Product Data Sheet (PDF)    
Purified Anti-Lck Antibody
3741505 25 µg $95.00       
3741510 100 µg $190.00       
Clone: LCK-01
Isotype: Mouse IgG1, κ
Reactivity: Human, does not cross-react with mouse
Immunogen: Peptide corresponding to a.a. 22-36 in human Lck
Formulation: This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide at 0.5 mg/ml.
Preparation: The antibody was purified by affinity chromatography.
Concentration: 0.5 mg/ml
Storage & Handling: The antibody solution should be stored undiluted between 2°C and 8°C.

WB - Quality tested
IF - Validated
IP, FC, ICC - Reported in the literature

Recommended Usage:

Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 5 µg per 5 ml antibody dilution buffer for each mini-gel. For immunofluorescence microscopy, a concentration range of 1-5 µg/ml is recommended. It is recommended that the reagent be titrated for optimal performance for each application.

Application References:

1. Romagnoli P, et al. 2001. Int. Immunol. 13:305.

Total cell lysate from Jurkat

Total cell lysate from Jurkat cells (lane 1, 15 µg), mouse thymus (lane 2, 15 µg) and HeLa cells (lane 3, 15 µg) were resolved by electrophoresis (4-20% Tris-Glycine gel), transferred to nitrocellulose, and probed with purified anti-Lck antibody (clone LCK-01). Proteins were visualized using an HRP Goat anti-mouse IgG Antibody and chemiluminescence detection. Direct-Blot™ HRP anti-β-actin antibody (clone 2F1-1) was used as a loading control.

Jurkat cells were fixed with

Jurkat cells were fixed with 4% PFA for ten minutes, permeabilized with 0.5% Triton X-100 for five minutes, and blocked with 5% FBS for 30 minutes. Then the cells were stained with 2 µg/mL anti-Lck Antibody (clone LCK-01) followed by Alexa Fluor® 594 (red) conjugated goat anti-mouse IgG in blocking buffer for two hours at room temperature. Nuclei were counterstained with DAPI (blue). The image was captured with a 60X objective.


Lck is a 56 kD tyrosine protein kinase and a member of the src subfamily that contains both an SH2 and SH3 domain. Alternatively spliced isoforms of Lck have been reported. Lck is a cytoplasmic protein bound to CD4 and CD8 in T lymphocytes that participates in antigen-induced T cell activation through phosphorylation of the T cell receptor zeta chain. Lck is activated upon T cell receptor engagement and is involved in the onset of cell cycle progression induced by interleukin-2. Phosphorylation by Csk downregulates the activity of Lck. In addition to CD4 and CD8, Lck has been reported to interact with PI3K through its SH3 domain and tyrosine phosphorylated KHDRBS1/p70 through its SH2 domain. In addition, Lck has been shown to associate with the SAP transmembrane tyrosine phosphatase. The Lck-01 monoclonal antibody recognizes human Lck and has been shown to be useful for Western blotting, immunoprecipitation, immunocytochemistry, and flow cytometry.

Other Names: Proto-oncogene tyrosine kinase lck, p56-Lck, T-cell specific protein tyrosine kinase< p56-LCK, LSK, T cell-specific protein-tyrosine kinase>
Structure: Belongs to the tyrosine family of kinases, src subfamily. Contains one SH2 domain, 1 SH3 domain. Approximately 56 kD, alternatively spliced isoforms have been reported
Distribution: Cytoplasmic protein, bound to cytoplasmic CD4 and CD8 in T lymphocytes
Function: Participates in antigen-induced T cell activation, phosphorylates zeta chain of T cell receptor. Involved in interleukin-2 induced onset of cell cycle progression
Regulation: Activated upon T cell receptor engagement. Tyrosine phosphorylation by p50 Csk downregulates catalytic activity
Modification: Phosphorylation
Interaction: Associates with CD4 and CD8 co-receptors. Binds to PI3K through SH3 interactions, binds to tyrosine phosphorylated KHDRBS1/p70 through SH2 domain. Interacts with SAP transmembrane tyrosine phosphatase
Antigen References:

1. Koga Y, et al. 1986. Eur. J. Immunol. 16:1643.
2. Vogel LB, et al. 1995. Biochem. Biophys. Acta 1264:168.
3. Vogel LB, et al. 1993. Mol. Cell. Biol. 13:7408.
4. Bergaman M, et al. 1992. EMBO J. 11:2919.