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.

Serine protease HTRA1 (EC 3.4.21.-) (High-temperature requirement A serine peptidase 1) (L56) (Serine protease 11)
HTRA1 HTRA PRSS11

Q92743

Human

WB

WB 1:500

51.3KD

Mouse

Human recombinant protein fragment of Human HTRA1 (NP_002766) produced in Ecoli.

Monoclonal

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at -20 °C. Stable for 12 months from date of receipt.