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SPPL2A encodes a member of the GXGD family of aspartic proteases, which are transmembrane proteins with two conserved catalytic motifs localized within the membrane-spanning regions, as well as a member of the signal peptide peptidase-like protease (SPPL) family. Additionally we are shipping SPPL2A Proteins (5) and many more products for this protein.
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Study propose that elements within the transmembrane segment and the luminal juxtamembrane domain facilitate intramembrane proteolysis of CD74 (show CD74 Antibodies) by SPPL2a.
In human B cells, SPPL2a is indispensable for turnover of CD74 (show CD74 Antibodies) N-terminal fragment. A human 15q21.2 microdeletion leads to loss of SPPL2a transcript and protein.
Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).
Data show that endogenous SPPL2a - in agreement with overexpression studies - is localised in membranes of lysosomes/late endosomes.
SPP (show SPEB Antibodies), SPPL2a, -2b, -2c, and -3 probably cleave type II-oriented substrate peptides as shown by consensus analysis
ADAM10 (show ADAM10 Antibodies) and SPPL2a were identified as two proteases implicated in FasL (show FASL Antibodies) processing and release of the FasL (show FASL Antibodies) intracellular domain, which has been shown to be important for retrograde FasL (show FASL Antibodies) signaling
SPPL2a and SPPL2b (show SPPL2B Antibodies) mediate the intramembrane cleavage, whereas neither SPP (show SPEB Antibodies) nor SPPL3 (show SPPL3 Antibodies) is capable of processing the Bri2 (show ITM2B Antibodies) N-terminal fragment.
SPPL2a-mediated processing of CD74 (show CD74 Antibodies) NTF (show TNF Antibodies) is indispensable to maintain appropriate levels of tonic BCR (show BCR Antibodies) signaling to promote B cell maturation (show TNFRSF17 Antibodies).
in vivo SPPL2a, but not SPPL2b (show SPPL2B Antibodies), exhibit a physiologically relevant contribution to CD74 (show CD74 Antibodies) proteolysis in B and dendritic cells
intramembrane proteolysis by SPPL2A is essential for maintaining cellular homeostasis of ameloblasts.
Sppl2a is required for B cell and dendritic cells development and survival.
Sppl2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain.
B cell survival and dendritic cells function requires SPPL2A.
This gene encodes a member of the GXGD family of aspartic proteases, which are transmembrane proteins with two conserved catalytic motifs localized within the membrane-spanning regions, as well as a member of the signal peptide peptidase-like protease (SPPL) family. This protein is expressed in all major adult human tissues and localizes to late endosomal compartments and lysosomal membranes. A pseudogene of this gene also lies on chromosome 15.
signal peptide peptidase-like 2A
, Signal peptide peptidase-like 2A
, SPP-like 2A
, intramembrane cleaving protease
, intramembrane protease 3
, presenilin-like protein 2
, SPP-like 2A protein
, protein SPPL2a