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MARCH1 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 126.96.36.199).
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MARCH1 functions as a tumor promoter by upregulating the NF-kappaB and the Wnt/b-catenin pathways, indicating that MARCH1 may be a therapeutic target for patients with ovarian cancer.
findings highlight the complex regulation of MARCH1 trafficking in the endocytic pathway as well as the intricate interactions between its cytoplasmic tails.
MARCH1 is capable of autoubiquitination, thus regulating its own expression.
expression of MARCH1 or MARCH8 (show MARCH8 Antibodies) causes a drastic change CD98 (show SLC3A2 Antibodies) trafficking after endocytosis
MARCH I is a major regulator of HLA-DR traffic, and its loss contributes to the acquisition of the potent immunostimulatory properties of mature human DCs.
The immunosuppressive effect of IL-10 on antigen presentation is mediated through induced expression of MARCH1.
We conclude that MARCH1 exerts MHCII-independent effects that regulate the innate arm of immunity
March-I ubiquitination prevents MHC class II recycling and promotes MHC class II turnover in antigen-presenting cells
IL-10 (show IL10 Antibodies) stimulates expression of the E3 ubiquitin ligase (show MUL1 Antibodies) March-I in activated macrophages, thereby down-regulating MHC-II, CD86 (show CD86 Antibodies), and antigen presentation to CD4 (show CD4 Antibodies) T cells.
Dendritic cells co-cultivated with antigen-specific induced Tregs expressed high levels of MARCH1. A major suppressive mechanism of DC function by iTregs is secondary to the effects of IL-10 (show IL10 Antibodies) on MARCH1 & CD83 (show CD83 Antibodies) expression.
DCs deficient in MARCH1 or MHCII ubiquitination both failed to generate antigen-specific T reg (show KCNH2 Antibodies) cells in vivo and in vitro.
aberrant degradation of spleen DCs MARCH1-mediated ubiquitinated proteins is involved during the earliest stage of MODS development.
IL-10 can have opposite effects on MARCH1 regulation in different cell types.
Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1).
found that the transmembrane domain of CD83 enhances MHC class II and CD86 expression by blocking MHC class II association with the ubiquitin ligase MARCH1
Selective ubiquitination of MHC-II in immature dendritic cells by the E3 ubiquitin ligase (show MUL1 Antibodies) March-I results in the selective degradation of internalized pMHC-II.
Study demonstrated the significant associations of genetic variants of the PDGFRB and MARCH1 genes with semen production traits.
MARCH1 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 188.8.131.52). MARCH proteins add ubiquitin (see MIM 191339) to target lysines in substrate proteins, thereby signaling their vesicular transport between membrane compartments. MARCH1 downregulates the surface expression of major histocompatibility complex (MHC) class II molecules (see MIM 142880) and other glycoproteins by directing them to the late endosomal/lysosomal compartment (Bartee et al., 2004
E3 ubiquitin-protein ligase MARCH1
, RING finger protein 171
, membrane-associated RING finger protein 1
, membrane-associated RING-CH protein I
, membrane-associated ring finger (C3HC4) 1