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The protein encoded by RHBDL2 is a member of the rhomboid family of integral membrane proteins. De plus, nous expédions RHBDL2 Protéines (4) et beaucoup plus de produits pour cette protéine.
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Human Polyclonal RHBDL2 Primary Antibody pour WB - ABIN2782918
Cheng, Wu, Lin, Hsu, Liu, Chang, Chen, Lai, Shi, Wu: Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing. dans The Journal of investigative dermatology 2011
Thrombomodulin and RHBDL2 are upr (Montrer THBD Anticorps)egulated in human HaCaT cells stimulated by scratch wounds; furthermore, increased solulbe thrombomodulin was found (Montrer THBD Anticorps) in culture medium.
RHBDL2 cleaves epidermal growth factor (Montrer EGF Anticorps) just outside its transmembrane domain, thereby facilitating its secretion and triggering activation of the epidermal growth factor receptor (Montrer EGFR Anticorps).
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 (Montrer EFNB2 Anticorps) and ephrin B3 (Montrer EFNB3 Anticorps).
RHBDL2 and soluble thrombomodulin (Montrer THBD Anticorps) were upregulated in ex vivo tissue culture of injured mouse skin. 3,4-Dichloroisocoumarin inhibited thrombomodulin (Montrer THBD Anticorps) production and wound healing; this was reversed by recombinant thrombomodulin (Montrer THBD Anticorps) 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