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
NOTCH1 antibody was raised against amino acids 2488-2502 from the C-Terminus of NOTCH1 (Human). A residue of cysteine was added to the amino terminal end to facilitate coupling.
Key Feature
Clonality
Polyclonal
Host Species
Rabbit
Tested Applications
ELISAIHCWB
NOTCH1 antibody can be used in ELISA starting at 1:000 - 1:1000, and immunohistochemistry starting at 5 μg/mL.: