Serine protease HTRA1 (HTRA1), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 23-480aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: QLSRAGRSAP LAAGCPDRCE PARCPPQPEH CEGGRARDAC GCCEVCGAPE GAACGLQEGP CGEGLQCVVP FGVPASATVR RRAQAGLCVC ASSEPVCGSD ANTYANLCQL RAASRRSERL HRPPVIVLQR GACGQGQEDP NSLRHKYNFI ADVVEKIAPA VVHIELFRKL PFSKREVPVA SGSGFIVSED GLIVTNAHVV TNKHRVKVEL KNGATYEAKI KDVDEKADIA LIKIDHQGKL PVLLLGRSSE LRPGEFVVAI GSPFSLQNTV TTGIVSTTQR GGKELGLRNS DMDYIQTDAI INYGNSGGPL VNLDGEVIGI NTLKVTAGIS FAIPSDKIKK FLTESHDRQA KGKAITKKKY IGIRMMSLTS SKAKELKDRH RDFPDVISGA YIIEVIPDTP AEAGGLKEND VIISINGQSV VSANDVSDVI KRESTLNMVV RRGNEDIMIT VIPEEIDP. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Serine protease with a variety of targets, including Extracellular domain matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the Extracellular domain space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. Reference: "Primary structure of a putative serine protease specific for IGF-binding proteins."Zumbrunn J., Trueb B.FEBS Lett. 398:187-192(1996). Function: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.