SPPL2b (signal peptide peptidase-like 2b), also known as PSL1 or IMP4 (intramembrane protease 4), is a 592 amino acid multi-pass membrane protein that contains one protease associated domain and belongs to the GXGD family of aspartic proteases. Localized to the membrane of the Golgi apparatus and to lysosomes, endosomes and the plasma membrane, SPPL2b functions as an intramembrane protease that specifically cleaves the transmembrane domain of TNFå. Once cleaved, TNFå releases its intracellular domain, thus triggering the immunity-related expression of cytokines (also known as interleukins) which are used in various pathways throughout the body. SPPL2b also interacts with and catalyzes the intramembrane proteolysis of ITM2B (integral membrane protein 2B), a protein that, when mutated, is associated with dementia. Four isoforms of SPPL2b exist due to alternative splicing events.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
recommended for detection of SPPL2b of human origin by WB, IP, IF, IHC(P) and ELISA: