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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 and many more products for this protein.
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Human Polyclonal SPPL2A Primary Antibody for IHC (p), ELISA - ABIN545831
Grigorenko, Moliaka, Korovaitseva, Rogaev: Novel class of polytopic proteins with domains associated with putative protease activity. in Biochemistry. Biokhimii?a 2002
inherited SPPL2a deficiency in humans underlies mycobacterial disease by decreasing the numbers of dendritic cells and impairing IFN-gamma production by mycobacterium-specific memory TH1* cells
Study propose that elements within the transmembrane segment and the luminal juxtamembrane domain facilitate intramembrane proteolysis of CD74 by SPPL2a.
In human B cells, SPPL2a is indispensable for turnover of CD74 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, SPPL2a, -2b, -2c, and -3 probably cleave type II-oriented substrate peptides as shown by consensus analysis
ADAM10 and SPPL2a were identified as two proteases implicated in FasL processing and release of the FasL intracellular domain, which has been shown to be important for retrograde FasL signaling
SPPL2a and SPPL2b mediate the intramembrane cleavage, whereas neither SPP nor SPPL3 is capable of processing the Bri2 N-terminal fragment.
Sppl2a-/- mice lack conventional dendritic cells, have CD4+ T cells that produce small amounts of IFN-gamma after BCG infection, and are highly susceptible to infection with BCG or Mycobacterium tuberculosis
SPPL2a-mediated processing of CD74 NTF is indispensable to maintain appropriate levels of tonic BCR signaling to promote B cell maturation.
in vivo SPPL2a, but not SPPL2b, exhibit a physiologically relevant contribution to CD74 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