SKU: PDEH100755_100μg-ES

Recombinant Human S100B protein(GST tag), 100 μg

Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. 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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Product Specification

Basic Information

Brands:Elabscience

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Place of Origin:China

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Sterile Status:

Reconstitution:It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.

Shipping:This product is provided as lyophilized powder which is shipped with ice packs.

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Calculated Molecular Weight:36.6 kDa

Observed Molecular Weight:37 kDa

Purity: > 90% as determined by reducing SDS-PAGE.

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Storage:Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

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Calculated Molecular Weight:36.6 kDa

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Endotoxin:< 10 EU/mg of the protein as determined by the LAL method.

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Research Areas:Cell Biology,Epigenetics and Nuclear Signaling,Stem Cells

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Bio-activity:Not validated for activity

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Formulation:Lyophilized from sterile PBS, pH 7.4.
Normally 5%-8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.

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