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  • 产品名称：Stathmin1(STMN1)(AA2-149)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
Stathmin1(STMN1)(AA2-149)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 18.1 kDa. The protein migrates as 17-20 kDa under reducing (R) condition (SDS-PAGE).
Purity >92 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
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.
Molecular Weight 18.1 kDa
NCBI Accession NP_981946
UniProt P16949
Research Area Signaling, Cytoskeleton, Alzheimer's Disease
Pathways MAPK Signaling, Microtubule Dynamics
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Stathmin 1 (STMN1) (AA 2-149) (Active) protein (His tag) (ABIN2181791) Human Stathmin 1, His Tag on SDS-PAGE under reducing (R) condition. The gel was stain...
Background publications Redeker, Lachkar, Siavoshian, Charbaut, Rossier, Sobel, Curmi: "Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry." in: The Journal of biological chemistry, Vol. 275, Issue 10, pp. 6841-9, 2000 (PubMed).