Anti-Signal peptide peptidase-like 3 Antibody, clone 7F9

Evaluated by Western Blotting in HEK293 cell lysate.

Western Blotting Analysis: 1 µg/mL of this antibody detected Signal peptide peptidase-like 3 in HEK293 cell lysate.

Anti-Signal peptide peptidase-like 3, clone 7F9, Cat. No. MABS1910, is a mouse monoclonal antibody that detects Signal peptide peptidase-like 3 and has been tested for use in Immunoprecipitation and Western Blotting.

Research Category
Signaling

Western Blotting Analysis: A representative lot detected Signal peptide peptidase-like 3 in Western Blotting applications (Voss, M., et. al. (2012). J Biol Chem. 287(52):43401-9; Voss, M., et. al. (2014). EMBO J. 33(24):2890-905; Fleck, D., et. al. (2016). J Biol Chem. 291(1):318-33).

Immunoprecipitation Analysis: A representative lot detected Signal peptide peptidase-like 3 in Immunoprecipitation applications (Voss, M., et. al. (2012). J Biol Chem. 287(52):43401-9).

Clone 7F9 detects Signal peptide peptidase-like 3 in human cells. it targets an epitope within 15 amino acids from the C-terminal half. Immunogen sequence is conserved in all three isoforms.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Signal peptide peptidase-like 3 (UniProt: Q8TCT6; also known as SPP-like 3, Intramembrane protease 2, IMP-2, Presenilin homologous protein 1, PSH1, Presenilin-like protein 4, SPPL3) is encoded by the SPPL3 (also known as IMP2) gene (Gene ID: 121665) in human. SPPL3 is a multi-pass transmembrane protein that is shown to be widely expressed and is highly conserved in multicellular eukaryotes. Three isoforms of SPPL3 have been described that are produced by alternative splicing. It is a member of the intramembrane-cleaving GxGD proteases. It acts as an intramembrane protease that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries. It can also act as a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifying glycosidases and glycosyltransferases. It is also shown to catalyze 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-mediated cleavage proteolysis. The first transmembrane domain of SPPL3 may act as a type I signal anchor. SPPL3 also contains a PAL motif (aa 342-344) that is required for normal active site conformation.

~42 kDa observed; 42.56 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

KLH-conjugated linear peptide corresponding to 15 amino acids from the C-terminal half of human Signal peptide peptidase-like 3.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G purified

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.