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Application: In vivo tyrosine phosphorylation of recombinant proteins for downstream applications.
Background: Tyrosine phosphorylation is a key regulatory mechanism in signal transduction pathways and plays a critical role in controlling protein activity, signaling, and stability. EphB1, a member of the Eph receptor tyrosine kinase family, catalyzes the transfer of a phosphate group from ATP to specific tyrosine residues on substrate proteins. EphB1-transformed competent E. coli cells express the cytoplasmic kinase domain of EphB1, allowing in vivo phosphorylation of recombinant target proteins that contain appropriate tyrosine residues or recognition motifs. This system enables the production of site-specific phosphorylated proteins in a prokaryotic host, eliminating the need for more complex eukaryotic systems. The result is an efficient method for generating homogeneous phosphoproteins suitable for downstream biochemical and structural studies.
Description: EphB1-Transformed Chemically Competent E. coli Cells are supplied in 10 x 50 µl vials in aqueous solution containing 10 mM sodium MOPS (pH 7.0), 75 mM CaCl2, 10 mM KCl, and 15% glycerol. Strain BL21(DE3), E. coli B strain with the DE3 lysogen, contains an IPTG (Isopropyl β-D-1-thiogalactopyranoside)-inducible EphB1 (Ephrin type-B receptor 1) expression plasmid maintained with streptomycin/spectinomycin. These cells are compatible with most cloning vectors and are suitable for the expression and in vivo tyrosine phosphorylation of recombinant proteins.
Host Cell Line: E. coli
Storage Stability: Cells are shipped in dry ice and should immediately be thawed or stored in liquid nitrogen upon receipt. Do not use a -80°C freezer for long term storage.
Target: EPHB1
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: BSL-1
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