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TRIM63 encodes a member of the RING zinc finger protein family found in striated muscle and iris. Additionally we are shipping TRIM63 Proteins (7) and TRIM63 Kits (4) and many more products for this protein.
Showing 10 out of 98 products:
Cow (Bovine) Polyclonal TRIM63 Primary Antibody for EIA, IHC (p) - ABIN782924
de Palma, Marinelli, Pavan, Orazi: Ubiquitin ligases MuRF1 and MAFbx in human skeletal muscle atrophy. in Joint, bone, spine : revue du rhumatisme 2008
Show all 3 references for ABIN782924
Human Polyclonal TRIM63 Primary Antibody for IP, WB - ABIN529746
Meinen, Lin, Rüegg, Punga: Fatigue and muscle atrophy in a mouse model of myasthenia gravis is paralleled by loss of sarcolemmal nNOS. in PLoS ONE 2012
Human Polyclonal TRIM63 Primary Antibody for ELISA, WB - ABIN185526
Cao, Kim, Lecker: Ubiquitin-protein ligases in muscle wasting. in The international journal of biochemistry & cell biology 2005
Human Polyclonal TRIM63 Primary Antibody for IHC, ELISA - ABIN184950
Dai, Liew: A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain. in The Journal of biological chemistry 2001
MuRF2 (show TRIM55 Antibodies) regulates PPARgamma1 activity to protect against diabetic cardiomyopathy and enhance weight gain induced by a high fat diet.
MuRF1 directly interacts with PPARalpha (show PPARA Antibodies), mono-ubiquitinates it, and targets it for nuclear export to inhibit fatty acid oxidation in a proteasome independent manner.
Increased Expression of MuRF1 Is Associated with Radiation-induced Laryngeal Muscle Atrophy.
MURF1 was upregulated in cancer cachexia mice.
Expression of USP19 (show USP19 Antibodies) correlates with that of MuRF1 and MAFbx/atrogin-1 (show FBXO32 Antibodies) in skeletal muscles
Sunitinib is able to restrain the overactivation of STAT3 (show STAT3 Antibodies) and MuRF-1 pathways, involved in enhanced muscle protein catabolism during cancer cachexia.
provide evidence that high CO2 activates skeletal muscle atrophy via AMPKalpha2 (show PRKAA2 Antibodies)-FoxO3a (show FOXO3 Antibodies)-MuRF1, which is of biological and potentially clinical significance in patients with lung diseases and hypercapnia
an atrophic role for MuRF1 regulating the magnitude of right ventricular hypertrophy
This data provides evidence for MuRF1 as a novel regulator of cardiac ROS (show ROS1 Antibodies), offering another mechanism by which increased MuRF1 expression may be cardioprotective in ischemia reperfusion injury.
Data reveal that Titin (show TTN Antibodies) protein is a pseudokinase with non-detectable catalytic output but is a high-affinity binding locus for MuRF1.
A novel protein aggregate myopathies and cardiomyopathy resulting from combined homozygous MuRF1 null mutation and heterozygous MuRF3 (show TRIM54 Antibodies) missense mutation.
Vitamin D3 might have an inhibitory effect on the expression of MAFbx (show FBXO32 Antibodies) and MuRF1 in skeletal muscle.
MURF1 expression intended to be increased in the skeletal muscle of patients with malignant disease even before cancer related cachexia weight loss.
TRIM63 gene expression involved in skin hyperpigmentation.
Skeletal muscle atrophy induced by Angiotensin II involves activation of MuRF1 expression.
These data strongly supported that rare variants in MuRF1 and MuRF2 (show TRIM55 Antibodies) are associated with higher penetrance and more severe clinical manifestations of hypertrophic cardiomyopathy.
In conclusion, atrogin-1 (show FBXO32 Antibodies), MuRF1, FOXO1 (show FOXO1 Antibodies)/3A, and eIF3 (show EIF3A Antibodies)-f mRNA, and protein levels, are differentially regulated by exercise contraction mode but not WPH supplementation combined with hypertrophy-inducing training.
both MuRF1 and MAFbx (show FBXO32 Antibodies) are enriched in skeletal, cardiac, and smooth muscle--REVIEW
This gene encodes a member of the RING zinc finger protein family found in striated muscle and iris. The product of this gene is an E3 ubiquitin ligase that localizes to the Z-line and M-line lattices of myofibrils. This protein plays an important role in the atrophy of skeletal and cardiac muscle and is required for the degradation of myosin heavy chain proteins, myosin light chain, myosin binding protein, and for muscle-type creatine kinase.
ring finger protein 29
, tripartite motif-containing protein 55
, muscle-specific RING finger protein 2
, tripartite motif-containing 63
, ring finger protein 30
, muscle specific ring finger protein 1
, E3 ubiquitin-protein ligase TRIM63
, muscle ring finger protein 1
, muscle specific RING finger protein-1
, e3 ubiquitin-protein ligase TRIM63-like
, tripartite motif containing 63
, iris ring finger protein
, muscle specific ring finger protein 2
, muscle-specific RING finger protein 1
, ring finger protein 28
, striated muscle RING zinc finger protein
, tripartite motif-containing protein 63
, tripartite motif protein 63