Synonyms	ALK1;ALP;BLPI;HUSI;HUSI-I;MPI;WAP4;WFDC4
Species	Human
Expression_host	Baculovirus-Insect Cells
Sequence	Met 1-Ala132
Accession	P03973
Mol_Mass	13.1 kDa
AP_Mol_Mass	15 kDa
Tag	C-His
Bio_Activity	Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK (Dnp)-NH2 (Catalog # ES002). The IC50 value is < 1 Nm.

Properties

Purity	> 90 % as determined by reducing SDS-PAGE.
Endotoxin level	< 1.0 EU per μg of the protein as determined by the LAL method.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.4 Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution	Please refer to the printed manual for detailed information.

Background

Secretory leukoprotease inhibitor (SLPI); also called antileukoprotease (ALP); is a 12-kDa; nonglycosylated serine protease inhibitor present in mucous secretions. It is thought to play a role in protecting the mucosae from injury associated with inflammation. SLPI is locally produced by serous cells; including bronchial submucosal glands. Elafin and SLPI are members of larger families of proteins secreted predominantly at mucosal sites; and have been shown to be modulated in multiple pathological conditions. Elafin and SLPI are structurally related in that both have a fold with a four-disulfide core or whey acidic protein (WAP) domain responsible for inhibiting proteases. SLPI is a prominent innate immune protein of the respiratory tract; possessing serine protease inhibitor activity; antibacterial activity; and anti-inflammatory/immunomodulatory activity.

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