Description
Recombinant Human Lacritin/LACRT Protein (His Tag) | PKSH032678 | Gentaur US, UK & Europe Disrtribition
Synonyms: Extracellular Glycoprotein Lacritin; LACRT
Active Protein: N/A
Activity: Recombinant Human Lacritin is produced by our E.coli expression system and the target gene encoding Ala19-Ala138 is expressed with a 6His tag at the N-terminus.
Protein Construction: Recombinant Human Lacritin is produced by our E.coli expression system and the target gene encoding Ala19-Ala138 is expressed with a 6His tag at the N-terminus.
Fusion Tag: N-6His
Species: Human
Expressed Host: E.coli
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and 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.
Molecular Mass: 14.6 kDa
Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Reconstitution: Please refer to the printed manual for detailed information.
Background: Extracellular glycoprotein lacritin (Lacritin) is a secreted protein which consists of 119 amino acids after cleavage of the N-terminal signal peptide and displays several predicted alpha helices, mostly in the C-terminal half. Lacritin is highly expressed in the lacrimal gland, localizes primarily to secretory granules and secretory fluid. Lacritin modulates lacrimal acinar cell secretion, promotes ductal cell proliferation, and stimulates signaling through tyrosine phosphorylation and release of calcium. Lacritin is thus a multifunctional prosecretory mitogen with cell survival activity. Natural or bacterial cleavage of lacritin releases a C-terminal fragment that is bactericidal. Lacritin cell targeting is dependent on the cell surface heparan sulfate proteoglycan syndecan-1 (SDC1). Binding utilizes an enzyme-regulated 'off-on' switch in which active epithelial heparanase (HPSE) cleaves off heparan sulfate to expose a binding site in the N-terminal region of syndecan-1's core protein.
Research Area: N/A
