Recombinant Rat S100B protein(His tag) | PKSR500007

Recombinant Rat S100B protein(His tag) | PKSR500007 | Gentaur US, UK & Europe Disrtribition

Synonyms: S-100 protein beta chain;S-100 protein subunit beta;S100 calcium-binding protein B

Active Protein: N/A

Activity: A DNA sequence encoding theRat S100B protein (P04631) (Ser2-Glu92 LVPRGF Ser2-Glu92) was expressed with a N-His.

Protein Construction: A DNA sequence encoding theRat S100B protein (P04631) (Ser2-Glu92 LVPRGF Ser2-Glu92) was expressed with a N-His.

Fusion Tag: N-His

Species: Rat

Expressed Host: E.coli

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

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

Endotoxin: Please contact us for more information.

Stability and 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.

Molecular Mass: 21.9 kDa

Formulation: Lyophilized from sterile PBS, pH 7.5, 5% trehalose, 5% mannitol, 0.01% tween-80.

Reconstitution: Please refer to the printed manual for detailed information.

Background: 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.

Research Area: N/A