|Other Names||Signal peptide peptidase-like 2B, SPP-like 2B, SPPL2b, 3423-, Intramembrane protease 4, IMP-4, Presenilin homologous protein 4, PSH4, Presenilin-like protein 1, SPPL2B, IMP4, KIAA1532, PSL1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6312b was selected from the Center region of human SPPL2b. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17965014, PubMed:19114711, PubMed:22194595). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952, PubMed:16829951). May play a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus processed leader peptide gp18 of the envelope glycoprotein gp130 dependently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852).|
|Cellular Location||Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein; Lumenal side Note=targeted through the entire secretory pathway to endosomes/lysosomes (PubMed:15998642)|
|Tissue Location||Expressed predominantly in adrenal cortex and mammary gland.|
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Provided below are standard protocols that you may find useful for product applications.
Signal peptide peptidase (SPP) is an aspartyl protease that mediates clearance of signal peptides by proteolysis within the endoplasmic reticulum (ER). Like presenilins, SPP contains a critical GXGD motif in its C-terminal catalytic center. Several presenilin homologues/SPP-like proteins (PSHs/SPPL) have been identified. Unlike the ER localization of SPP and other SPPL proteins, SPPL2b is targeted through the secretory pathway to endosomes/lysosomes.
Friedmann, E., et al., J. Biol. Chem. 279(49):50790-50798 (2004).Grigorenko, A.P., et al., Biochemistry Mosc. 67(7):826-835 (2002).Weihofen, A., et al., Science 296(5576):2215-2218 (2002).
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