protein

S100A13 Protein, Human

HY-P71271

10 μg;50 μg

105;290 USD

S100A13 Protein, Human

proteins

E. coli

10 μg;50 μg

105;290 USD

The S100A13 protein is critical for unconventional protein export, binding calcium and copper ions without interference. It is essential for copper-dependent stress-induced export of IL1A and FGF1. S100A13 Protein, Human is the recombinant human-derived S100A13 protein, expressed by E. coli , with tag free. The total length of S100A13 Protein, Human is 97 a.a., with molecular weight of ~12.0 kDa.

Human

S100A13, a versatile protein, plays a pivotal role in the unconventional export of proteins devoid of a signal peptide. This function is orchestrated by its ability to bind two calcium ions per subunit and one copper ion, with the binding of copper not impeding calcium binding. Notably, S100A13 is indispensable for the copper-dependent stress-induced export of IL1A and FGF1. In a calcium-free state, the protein exhibits an affinity for lipid vesicles containing phosphatidylserine, distinguishing its membrane-interaction preferences. Structurally, S100A13 forms homodimers and is a constituent of a copper-dependent multiprotein complex alongside FGF1 and SYT1. These intricate interactions underscore the regulatory role of S100A13 in mediating the export of specific proteins through alternative pathways, contributing to cellular homeostasis. Additionally, the protein engages in direct interactions with IL1A, further expanding its repertoire of molecular partnerships.

Protein S100-A13; S100A13; S100 calcium-binding protein A13

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCl, 1mM CaCl 2 , 0.1% Tween-20, pH 8.0.

Room temperature in continental US;may vary elsewhere.