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P31151-Human S100A7-3d structure.jpg P31151-Human S100A7-3d structure.jpg

Human S100A7+SDS-PAGE.jpg Human S100A7+SDS-PAGE.jpg Greater than 95% as determined by reducing SDS-PAGE.

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

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Recombinant Human S100A7 is a human-derived protein expressed in E. coli as an untagged form. It belongs to the EF-hand calcium-binding protein family within the S100 family, with a molecular weight of approximately 11–12 kDa and N-terminal acetylation. This protein can bind both calcium and zinc ions. It is upregulated in lesional skin of psoriasis and atopic dermatitis, as well as in various epithelial cells. S100A7 exhibits zinc-binding-mediated antibacterial activity, induces upregulation of tight junction proteins to maintain epithelial integrity, and interacts with RAGE to promote immune cell migration and macrophage infiltration into tumor sites.

Synonyms: Recombinant Human S100A7; Protein S100-A7; Psoriasin

4.5 *For Research Use Only! Not for Human Use. We Do Not Sell to Patients.

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Product Details of Human S100A7

M.W : 11.5 KDa
SMILES Code : NONE
Synonyms :
Recombinant Human S100A7; Protein S100-A7; Psoriasin
English Name :Recombinant Human S100A7

Safety of Human S100A7

Isoform Comparison

Biological Activity

Description
S100A7 is a 11-12 kDa member of the S100 family of EF hand calcium binding proteins. Human S100A7 shares 32% amino acid sequence identity with mouse S100A7A, the closest related protein in mouse. It is acetylated at the N-terminus and binds both calcium and zinc ions. S100A7 is up-regulated in keratinocytes of psoriasis and atopic dermatitis lesions, as well as in epithelial cells of the tongue, eye, and female genital tract. Its up-regulation can be induced by bacterial exposure, inflammatory cytokines, or epidermal barrier disruption. S100A7 supports epithelial integrity through killing E. coli by sequestration of zinc and through inducing the up-regulation of tight junction proteins. The interaction of S100A7 with RAGE promotes the migration of immune cells and the infiltration of macrophages into tumor sites.
 

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