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The protein encoded by MID1 is a member of the tripartite motif (TRIM) family, also known as the 'RING-B box-coiled coil' (RBCC) subgroup of RING finger proteins. Additionally we are shipping MID1 Proteins (9) and MID1 Kits (7) and many more products for this protein.
Showing 10 out of 59 products:
Chicken Polyclonal MID1 Primary Antibody for WB - ABIN2775948
Winter, Lehmann, Krauss, Trockenbacher, Kijas, Foerster, Suckow, Yaspo, Kulozik, Kalscheuer, Schneider, Schweiger: Regulation of the MID1 protein function is fine-tuned by a complex pattern of alternative splicing. in Human genetics 2004
Human Polyclonal MID1 Primary Antibody for WB - ABIN439762
Bell, Malyukova, Holien, Koach, Parker, Kavallaris, Marshall, Cheung: TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members. in PLoS ONE 2012
Human Monoclonal MID1 Primary Antibody for ELISA, WB - ABIN517934
Liu, Knutzen, Krauss, Schweiger, Chiang: Control of mTORC1 signaling by the Opitz syndrome protein MID1. in Proceedings of the National Academy of Sciences of the United States of America 2011
Human Polyclonal MID1 Primary Antibody for WB - ABIN657388
Need, Attix, McEvoy, Cirulli, Linney, Hunt, Ge, Heinzen, Maia, Shianna, Weale, Cherkas, Clement, Spector, Gibson, Goldstein: A genome-wide study of common SNPs and CNVs in cognitive performance in the CANTAB. in Human molecular genetics 2009
we show that MID1 controls exocytosis of lytic granules and cytotoxicity in murine cytotoxic lymphocytes
X-linked microtubule-associated protein (show SPAG5 Antibodies), Mid1, regulates axon development.
MID1 inhibition also limited rhinovirus-induced exacerbation of allergic airway disease
Thus, lack of Mid1 causes a misspecification of the midbrain/cerebellar boundary that results in an abnormal development of the most anterior cerebellar lobes.
Analysis of Mid1, Hccs (show HCCS Antibodies), Arhgap6 (show ARHGAP6 Antibodies), and Msl3l1 (show MSL3 Antibodies) in X-linked polydactyly (Xpl) and Patchy-fur (Paf (show KIAA0101 Antibodies)) mutant mice
A130T/V mutations within the MID1 zinc-binding Bbox1 (show BBOX1 Antibodies) domain affects protein folding.
MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 (show BBOX1 Antibodies) domain disrupt polyubiquitination of alpha4 but not of PP2Ac (show PPP2CA Antibodies) in X-linked Opitz syndrome.
TRAIL regulates MID1 and TSLP (show TSLP Antibodies), inflammation, fibrosis, smooth muscle hypertrophy, and expression of inflammatory effector chemokines and cytokines in experimental eosinophilic esophagitis.
These studies provide insight into the mechanism by which mutations observed in X-linked Opitz G syndrome affect the structure and function of the MID1 Bbox1 (show BBOX1 Antibodies) domain
A familial c.1102C>T (p.R368X) mutation in the MID1 gene, is reported.
Results revealed S422 as a novel phosphorylation site of Osx and GSK-3b played an important role in regulating the protein stability and transactivational activity of Osx.
Fu ubiquitination and cleavage is one of the key elements connecting the MID1-PP2A (show PPP2R4 Antibodies) protein complex with GLI3 (show GLI3 Antibodies) activity control
Promotion of AR, in addition to enhancement of the Akt (show AKT1 Antibodies)-, NFkappaB (show NFKB1 Antibodies)-, and Hh-pathways by sustained MID1-upregulation during androgen deprivation therapy provides a powerful proliferative scenario for PCa (show FLVCR1 Antibodies) progression into castration resistance
In prostate cancer cells the inhibitory effect of metformin was mimicked by disruption of MID1 translational regulator complex.
Two patients with underdeveloped arcuate fasciculus had novel, nonsynonymous variants in MID1 and EN2 (show EN2 Antibodies) genes regulating axon guidance pathway.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also known as the 'RING-B box-coiled coil' (RBCC) subgroup of RING finger proteins. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein forms homodimers which associate with microtubules in the cytoplasm. The protein is likely involved in the formation of multiprotein structures acting as anchor points to microtubules. Mutations in this gene have been associated with the X-linked form of Opitz syndrome, which is characterized by midline abnormalities such as cleft lip, laryngeal cleft, heart defects, hypospadias, and agenesis of the corpus callosum. This gene was also the first example of a gene subject to X inactivation in human while escaping it in mouse. Multiple different transcript variants are generated by alternate splicing\; however, the full-length nature of some of the variants has not been determined.
, tripartite motif-containing protein 18
, RING finger protein 59
, midline 1 RING finger protein
, putative transcription factor XPRF
, tripartite motif protein TRIM18
, zinc finger on X and Y, mouse, homolog of
, Finger on X and Y (in rat only on X)