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Human S100B Protein  pdf  pdf  pdf


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S1B-H5143-100ug
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Synonym

S100B,NEF, S100, S100beta

Source

Recombinant Human S100B Protein (rh S100B) Met 1 - Glu 92 (Accession # NP_006263) was produced in E.coli cells at ACROBiosystems.

Molecular Characterization

rh S100B is fused with a polyhistidine tag at the N-terminus, and has a calculated MW of 11.5 kDa. The predicted N-terminus is Met. DTT-reduced Protein migrates as 11 kDa in SDS-PAGE .

Endotoxin

Less than 1.0 EU per μg of the rh S100B by the LAL method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl,pH8.0. 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 S100B Protein
The purity of rh S100B was determined by DTT-reduced (+) SDS-PAGE and staining overnight with Coomassie Blue.
 
 
 

Background

S-100 protein beta chain (S100B),a member of the S-100 family, is also known as S-100 protein subunit beta and S100 calcium-binding protein B, which contains two EF-hand domains. S100B can weakly bind calcium but bind zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Also, S100B can bind to and initiate the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction,S100B may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Fuethermore,S100B could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. S100B may mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.

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References