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The protein encoded by RHBDL2 is a member of the rhomboid family of integral membrane proteins. Additionally we are shipping RHBDL2 Antibodies (22) and many more products for this protein.
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Thrombomodulin and RHBDL2 are upr (show THBD Proteins)egulated in human HaCaT cells stimulated by scratch wounds; furthermore, increased solulbe thrombomodulin was found (show THBD Proteins) in culture medium.
RHBDL2 cleaves epidermal growth factor (show EGF Proteins) just outside its transmembrane domain, thereby facilitating its secretion and triggering activation of the epidermal growth factor receptor (show EGFR Proteins).
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 (show EFNB2 Proteins) and ephrin B3 (show EFNB3 Proteins).
RHBDL2 and soluble thrombomodulin (show THBD Proteins) were upregulated in ex vivo tissue culture of injured mouse skin. 3,4-Dichloroisocoumarin inhibited thrombomodulin (show THBD Proteins) production and wound healing; this was reversed by recombinant thrombomodulin (show THBD Proteins) 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