Recombinant Human htrA1 (mutated S328A) protein (His tag)
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Recombinant Human htrA1 (mutated S328A) protein (His tag) is a Human Fragment protein, in the 161 to 379 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
HTRA, PRSS11, HTRA1, Serine protease HTRA1, High-temperature requirement A serine peptidase 1, L56, Serine protease 11
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human htrA1 (mutated S328A) protein (His tag) (AB268648)
SDS-PAGE analysis of ab268648.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
HtrA1 participates in cellular processes including protein degradation and modulation of signaling pathways. It does not have a known direct association with protein complexes but its protease activity affects extracellular matrix components and influences cellular homeostasis. HtrA1's regulatory function can affect cell growth and differentiation impacting tissue development and repair mechanisms.
Pathways
HtrA1 interacts significantly with the TGF-beta signaling pathway where its protease activity modulates the availability and activity of TGF-beta ligands and receptors. It also plays a role in the Wnt signaling pathway by influencing the stability of pathway-related proteins. HtrA1 interacts with proteins such as TGF-beta contributing to the regulation of extracellular matrix and cellular responses to external signals.
Specifications
Form
Liquid
General info
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.
Sequence similarities
Belongs to the peptidase S1C family.
Target data
Product promise
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