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Human Stathmin 1 / STMN1 Protein  pdf  pdf  pdf


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Synonym

STMN1,Stathmin,C1orf215,LAP18,OP18

Source

Recombinant Human STMN1 /Stathmin Protein (rh STMN1 / Stathmin) Ala 2 - Asp 149 (Accession # NP_981946) was produced in E.coli cells at ACROBiosystems.

Molecular Characterization

rh STMN1 / Stathmin is fused with a polyhistidine tag at the N-terminus, and has a calculated MW of 18.1 kDa. The predicted N-terminus is Met. DTT-reduced Protein migrates as 17-20 kDa in SDS-PAGE .

Endotoxin

Less than 1.0 EU per μg of the rh STMN1 / Stathmin by the LAL method.

Purity

>92% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

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Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).

 

SDS-PAGE


Recombinant Human STMN1 /Stathmin Protein
The purity of rh STMN1 / Stathmin was determined by DTT-reduced (+) SDS-PAGE and staining overnight with Coomassie Blue.
 
 

Background

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.

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References

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