Recombinant Human S100A15 His-tag Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant Human S100A15 (Catalog # 11804-SA)
binds to Human S100A15 Antibody with an ED50 of <500 ng/mL. |
| Source |
E. coli-derived human S100A7A protein Ser2 - Gln101, with an N-terminal His tag |
| N-terminal Sequence |
His |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
11 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| SDS-PAGE |
11-13 kDa, under reducing conditions. |
Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 2 weeks, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
| Buffer |
Lyophilized from a 0.2 μm filtered solution in Tris with Trehalose. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 250 μg/mL in water. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human S100A15 His-tag Protein, CF
Background
S100 calcium‑binding protein A15 (S100A15), also known as
koebnerisin, is a small (~11 kDa) member of the S100 family of EF‑hand proteins
encoded within the epidermal differentiation complex on chromosome 1q21.
S100A15 emerged through primate‑specific gene duplication and is highly
homologous (>90% sequence identity) to S100A7 (psoriasin), yet displays
distinct regulation, cellular distribution, and biological function (1).
S100A15 is predominantly expressed in stratified squamous
epithelia, including the skin and mucosal surfaces, and is markedly upregulated
in inflammatory skin disorders such as psoriasis, particularly in koebnerized
lesions. Functionally, S100A15 acts as an innate immune alarmin and
antimicrobial peptide, contributing to epithelial barrier defense and immune
cell recruitment during inflammation (2, 3). Unlike many classical S100
proteins, S100A15 exhibits context‑dependent extracellular signaling activity that
promotes chemotaxis and cytokine production in immune cells.
Extracellular S100A15 functions as a pro‑inflammatory
mediator, stimulating leukocyte migration and amplifying local inflammatory
responses through receptor pathways that are distinct from those used by its
paralog S100A7. While S100A7 signals via the receptor for advanced glycation
end products (RAGE), S100A15 primarily acts through a Gi‑protein‑coupled
receptor pathway, enabling synergistic yet nonredundant pro‑inflammatory
signaling in epithelial tissues (4). This functional divergence allows the
S100A7/S100A15 subfamily to fine‑tune immune responses at sites of tissue
stress or damage.
Beyond inflammatory disease, dysregulated S100A15 expression
has been implicated in epithelial carcinogenesis, where it participates in
shaping the tumor microenvironment through immune modulation, chemotactic
signaling, and epithelial–immune crosstalk. Depending on cellular context,
S100A15 may support chronic inflammation that promotes tumor progression or
serve as a marker of epithelial immune activation (1, 5).
Recombinant human S100A15 is therefore a
valuable research tool for studying innate immunity, epithelial barrier
biology, inflammatory signaling, alarmin function, and cancer‑associated
inflammation, as well as for dissecting functional differences within the
closely related S100A7/A15 protein subfamily.
- Wolf, R. et al. (2010) Amino Acids 41:789.
- Hattinger, E. et al. (2013) Curr. Opin.
Pharmacol. 13:588.
- Kurpet, K. et al. (2022) Molecules 27:6640.
- Wolf, R. et al. (2008) J. Immunol. 181:1499.
- Liang, H. et al. (2023) Front. Immunol. 14:1191645.
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