The SPPL3 Polyclonal Antibody (PAC048706) is a valuable tool for researchers studying SPPL3, a key enzyme involved in intramembrane proteolysis. Raised in rabbits, this antibody is highly specific and reactive with human samples, making it ideal for use in Western blot applications. By binding to the SPPL3 protein, this antibody allows for the detection and analysis of SPPL3 in various cell types, facilitating research in the fields of immunology and neurobiology.SPPL3 is a critical player in the processing of membrane proteins, with implications for various cellular processes including signal transduction and protein trafficking.
Dysregulation of SPPL3 has been linked to neurodegenerative diseases and immune disorders, making it a promising target for therapeutic interventions. By elucidating the role of SPPL3 in these pathways, researchers can gain valuable insights into disease mechanisms and potential treatment strategies.
Immunofluorescent analysis of HepG2 cells using PACO48706 at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
Western Blot. Positive WB detected in: Hela whole cell lysate, HepG2 whole cell lysate, Jurkat whole cell lysate, MCF-7 whole cell lysate. All lanes: SPPL3 antibody at 3µg/ml. Secondary. Goat polyclonal to rabbit IgG at 1/50000 dilution. Predicted band size: 43, 19 kDa. Observed band size: 43 kDa.
Background:
Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries. Acts like a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifiying glycosidase and glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1. Catalyzes the intramembrane cleavage of the envelope glycoprotein gp130 and/or the leader peptide gp18LP of the simian foamy virus independent of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis. May also have the ability to serve as a shedding protease for subsequent intramembrane proteolysis by SPPL2A and SPPL2B of the envelope glycoprotein gp130. Plays a role in the regulation of cellular glycosylation processes. Required to link T-cell antigen receptor (TCR) and calcineurin-NFAT signaling cascades in lymphocytes by promoting the association of STIM1 and ORAI1 during store-operated calcium entry (SOCE) in a protease-independent manner.
Synonyms:
Signal peptide peptidase-like 3 (SPP-like 3) (EC 3.4.23) (Intramembrane protease 2) (IMP-2) (Presenilin homologous protein 1) (PSH1) (Presenilin-like protein 4), SPPL3, IMP2 PSL4
UniProt Protein Function:
SPPL3: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Belongs to the peptidase A22B family. 3 isoforms of the human protein are produced by alternative splicing.Protein type: Membrane protein, multi-pass; EC 3.4.23.-; Protease; Membrane protein, integralChromosomal Location of Human Ortholog: 12q24.31Cellular Component: rough endoplasmic reticulumMolecular Function: protein homodimerization activity; aspartic endopeptidase activity, intramembrane cleavingBiological Process: membrane protein ectodomain proteolysis
