SPINK5 (serine protease inhibitor Kazal-type 5) is a secreted multi-domain serine protease inhibitor. It is expressed in hair follicles in the inner root sheets and in the epidermis in the granular layer. This protein contains 15 serine protease inhibitor domains. It is composed of 1064 amino acids, and has a signal peptide. It is synthesized as a pro-protein, which is cleaved into different isoforms. Three isoforms of this protein exist- a short isoform with only the first 13 domains, the 15 domain isoform, and a long isoform with a 30 amino acid stretch inserted between domains 13 and 14. The molecular weight of 15 domain isoform is ~120kDa. SPINK5 gene is localized to human chromosome 5q32, and is made of 33 exons.
Synonyms: Anti-LEKTI antibody produced in rabbit; Anti-Lympho-epithelial Kazal-type-related inhibitor antibody produced in rabbit; Anti-Serine protease inhibitor Kazal-type 5 precursor antibody produced in rabbit
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: SPINK5 (serine protease inhibitor Kazal-type 5) inactivates kallikrein (KLK)5, KLK7, and KLK14, which are epidermal proteases. KLKs are proteases related to desquamation, and SPINK5 is involved in the negative regulation of KLKs, as well as other proteases. Therefore, for normal skin barrier function and desquamation, a balance between KLKs and SPINK5 is essential. Mutations in this gene are associated with Comèl-Netherton syndrome, which is an autosomal recessive disorder. It is characterized by abnormalities in the hair shaft, congenital ichthyosis, and atopic diathesis. Loss of SPINK5 activity leads to increased corneodesmosomal component desmoglein-1 (DSG1) degradation, resulting in aberrant stratum corneum detachment. SPINK5 420K variant is responsible for changes in the proteolytic activation of SPINK5, which increases the likelihood of atopic dermatitis.
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