Human Stathmin 1, His Tag (ST1-H5149) is expressed from E.coli cells. It contains AA Ala 2 - Asp 149 (Accession # NP_981946).
Predicted N-terminus: Met
This protein carries a polyhistidine tag at the N-terminus.
The protein has a calculated MW of 18.1 kDa. The protein migrates as 18 kDa under reducing (R) condition (SDS-PAGE).
Less than 1.0 EU per μg by the LAL method.
>92% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
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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 avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human Stathmin 1, 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 92%.
Stathmin (STMN1), a member of the stathmin family, is also known as Leukemia-associated phosphoprotein p18, Oncoprotein 18 (Op18), Phosphoprotein p19 (pp19), Protein Pr22 and pp17, which contains one SLD (stathmin-like) domain. The function of STMN1 as an important regulatory protein of microtubule dynamics has been well-characterized. Stathmin (STMN1) interacts with two molecules of dimeric α,β-tubulin to form a tight ternary complex called the T2S complex.One mole of STMN1 binds to two moles of tubulin dimers through the stathmin-like domain (SLD).When STMN1 sequesters tubulin into the T2S complex, tubulin becomes non-polymerizable. Without tubulin polymerization, there is no microtubule assembly.STMN1 also promotes microtubule disassembly by acting directly on the microtubule ends.