Notch is synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase (S1 cleavage) in the trans-golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved (S2 cleavage) by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin-dependent gamma-secretase (S3 cleavage) to release the intracellular domain (NICD) from the membrane.
Immunogen
NOTCH2 antibody was raised against amino acids from the C-Terminus of NOTCH2 (Human).
Key Feature
Clonality
Polyclonal
Host Species
Rabbit
Tested Applications
ELISAIHC
NOTCH2 antibody can be used in immunohistochemistry starting at 20 μg/mL.: