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The protein encoded by RHBDL2 is a member of the rhomboid family of integral membrane proteins. Zusätzlich bieten wir Ihnen RHBDL2 Proteine (4) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal RHBDL2 Primary Antibody für WB - ABIN2782918
Cheng, Wu, Lin, Hsu, Liu, Chang, Chen, Lai, Shi, Wu: Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing. in The Journal of investigative dermatology 2011
Thrombomodulin and RHBDL2 are upr (zeige THBD Antikörper)egulated in human HaCaT cells stimulated by scratch wounds; furthermore, increased solulbe thrombomodulin was found (zeige THBD Antikörper) in culture medium.
RHBDL2 cleaves epidermal growth factor (zeige EGF Antikörper) just outside its transmembrane domain, thereby facilitating its secretion and triggering activation of the epidermal growth factor receptor (zeige EGFR Antikörper).
Substrate specificity of RHBDL2 intramembrane protease is governed by helix-breaking residues in the transmembrane domain.
Here, the authors show that RHBDL2 is produced as a proenzyme and that the processing of RHBDL2 is required for its cellular protease activity.
The encoded protein is thought to release soluble growth factors by proteolytic cleavage of certain membrane-bound substrates, including ephrin B2 (zeige EFNB2 Antikörper) and ephrin B3 (zeige EFNB3 Antikörper).
RHBDL2 and soluble thrombomodulin (zeige THBD Antikörper) were upregulated in ex vivo tissue culture of injured mouse skin. 3,4-Dichloroisocoumarin inhibited thrombomodulin (zeige THBD Antikörper) production and wound healing; this was reversed by recombinant thrombomodulin (zeige THBD Antikörper) in mice.
The protein encoded by this gene is a member of the rhomboid family of integral membrane proteins. This family contains proteins that are related to Drosophila rhomboid protein. Members of this family are found in both prokaryotes and eukaryotes and are thought to function as intramembrane serine proteases. The encoded protein is thought to release soluble growth factors by proteolytic cleavage of certain membrane-bound substrates, including ephrin B2 and ephrin B3.
rhomboid (veinlet, Drosophila)-like 2
, rhomboid protease 2
, rhomboid-like protein 2
, rhomboid-related protein 2