protein

S100A13 Protein, Mouse (N-His)

HY-P76583A

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

35;60;170;290;950;1520 USD

S100A13 Protein, Mouse (N-His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

35;60;170;290;950;1520 USD

S100A13 Protein, acting as a homodimer, facilitates the export of signal peptide-lacking proteins through an alternative pathway, binding two calcium ions and one copper ion per subunit. It is crucial for the copper-dependent stress-induced export of IL1A and FGF1, with the calcium-free form binding to phosphatidylserine-containing lipid vesicles. S100A13 is part of a copper-dependent multiprotein complex, interacting with FGF1, SYT1, and IL1A. S100A13 Protein, Mouse (N-His) is the recombinant mouse-derived S100A13 protein, expressed by E. coli , with N-His labeled tag. The total length of S100A13 Protein, Mouse (N-His) is 98 a.a., with molecular weight of ~12 kDa.

Mouse

The S100A13 protein plays a crucial role in the export of proteins that lack a signal peptide and are secreted through an alternative pathway. It has the ability to bind two calcium ions per subunit and one copper ion, with the binding of the latter not interfering with calcium binding. S100A13 is essential for the copper-dependent stress-induced export of IL1A and FGF1. Interestingly, the calcium-free form of the protein can bind to lipid vesicles containing phosphatidylserine but not those containing phosphatidylcholine. S100A13 functions as a homodimer and is part of a copper-dependent multiprotein complex alongside FGF1 and SYT1. It also interacts with FGF1, SYT1, and IL1A.

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

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

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.