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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 Antibodies (58) and MID1 Kits (7) and many more products for this protein.
Showing 7 out of 9 products:
we show that MID1 controls exocytosis of lytic granules and cytotoxicity in murine cytotoxic lymphocytes
X-linked microtubule-associated protein (show SPAG5 Proteins), 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 Proteins), Arhgap6 (show ARHGAP6 Proteins), and Msl3l1 (show MSL3 Proteins) in X-linked polydactyly (Xpl) and Patchy-fur (Paf (show KIAA0101 Proteins)) mutant mice
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 Proteins) domain affects protein folding.
MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 (show BBOX1 Proteins) domain disrupt polyubiquitination of alpha4 but not of PP2Ac (show PPP2CA Proteins) in X-linked Opitz syndrome.
TRAIL regulates MID1 and TSLP (show TSLP Proteins), 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 Proteins) 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 Proteins) protein complex with GLI3 (show GLI3 Proteins) activity control
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)