The S100A13 protein is part of the S100 family of proteins, which includes two EF-hand calcium-binding motifs. It is abundantly expressed in a variety of tissues, with the highest expression level seen in the thyroid gland. This protein is also detected in smooth muscle cells, where it co-exists with other family members in the nucleus and stress fibers. It is involved in the export of proteins that lack a signal peptide and are produced by an alternative pathway. It links two calcium ions and one copper ion together in each subunit. Binding of one copper ion does not interfere with calcium binding. S100A13 is required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not those containing phosphatidylcholine. Human S100A13 Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.
Product Name:
Human S100A13 Recombinant Protein (RPES3209)
Product Code:
RPES3209
Size:
10µg
Species:
Human
Expressed Host:
E.coli
Synonyms:
Protein S100-A13,S100A13,S100 calcium-binding protein A13
Accession:
NP_001019381.1
Sequence:
Ala2-Lys98
Fusion tag:
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
Protein Construction:
Recombinant Human Protein S100-A13 is produced by our E.coli expression system and the target gene encoding Ala2-Lys98 is expressed.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
11.3 kDa
AP Mol Mass:
29 kDa
Formulation:
Lyophilized from a 0.2 µm filtered solution of 20mM PB?150mM NaCl,pH7.4.
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
system_update_altDatasheetMouse S100A13 Recombinant Protein S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding mo