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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 (8) and many more products for this protein.
Showing 10 out of 58 products:
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 - 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
identified four miRNAs, miR (show MLXIP Antibodies)-19, miR (show MLXIP Antibodies)-340, miR (show MLXIP Antibodies)-374 and miR (show MLXIP Antibodies)-542 that bind to the 3'-UTR (show UTS2R Antibodies) of the MID1 mRNA. These miRNAs not only regulate MID1 expression but also mTOR (show FRAP1 Antibodies) signaling and translation of disease associated mRNAs and could therefore serve as potential drugs for future therapy development
Our data reveal a novel role for MID1 and for atypical ubiquitination in balancing BRAF35 (show HMG20B Antibodies) presence, and likely its activity, within nuclear and cytoplasmic compartments
high levels of APNG (show MPG Antibodies) were associated with better overall survival in patients with glioblastoma
Data indicate that DNA glycosylases MYH (show MUTYH Antibodies), UNG2 (show CCNO Antibodies), MPG (show MPG Antibodies), NTH1, NEIL1 (show NEIL1 Antibodies), 2 and 3 on nascent DNA.
Data suggest that the change in tryptophan fluorescence of Y162W mutant of AAG (show MPG Antibodies) (alkyladenine DNA glycosylase) is extremely rapid upon binding to either damaged or undamaged DNA, much faster than lesion-recognition and nucleotide flipping steps; thus, intercalation by tyrosine may be one of the earliest steps in search for/recognition of DNA damage.
P151L MID1 mutation is associated with X-linked Opitz Syndrome.
the coiled-coil and COS domain (CC-COS) bind to microtubules, demonstrating for the first time that MID1 can directly associate with the microtubules
Osx is upregulated in patients with Ossification of the posterior longitudinal ligament.
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.
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
SHH (show SHH Antibodies)-dependent E-ligase Midline1 regulates ubiquitin-mediated proteasomal degradation of Pax6 (show PAX6 Antibodies) during visual system development.
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.
RING finger protein 59
, midline 1 RING finger protein
, putative transcription factor XPRF
, tripartite motif protein TRIM18
, tripartite motif-containing protein 18
, zinc finger on X and Y, mouse, homolog of
, Finger on X and Y (in rat only on X)
, E3 ubiquitin-protein ligase Midline-1
, midline 1 (Opitz/BBB syndrome)