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SMN1 is part of a 500 kb inverted duplication on chromosome 5q13. Additionally we are shipping SMN1 Kits (31) and SMN1 Proteins (8) and many more products for this protein.
Showing 10 out of 104 products:
Mouse (Murine) Monoclonal SMN1 Primary Antibody for ICC, FACS - ABIN108567
Liu, Dreyfuss: A novel nuclear structure containing the survival of motor neurons protein. in The EMBO journal 1996
Show all 2 references for ABIN108567
Human Polyclonal SMN1 Primary Antibody for IHC, ELISA - ABIN1585252
Smith, Kuliszewski, Liao, Rudenko, Stewart, Leong-Poi: Sustained improvement in perfusion and flow reserve after temporally separated delivery of vascular endothelial growth factor and angiopoietin-1 plasmid deoxyribonucleic acid. in Journal of the American College of Cardiology 2012
Dog (Canine) Polyclonal SMN1 Primary Antibody for WB - ABIN2778671
Hirano, Angelini, Montagna, Hays, Tanji, Mitsumoto, Gordon, Naini, DiMauro, Rowland: Amyotrophic lateral sclerosis with ragged-red fibers. in Archives of neurology 2008
Human Monoclonal SMN1 Primary Antibody for ICC, IHC - ABIN969408
Hendrickson, Donohoe, Akmaev, Sugarman, Labrousse, Boguslavskiy, Flynn, Rohlfs, Walker, Allitto, Sears, Scholl: Differences in SMN1 allele frequencies among ethnic groups within North America. in Journal of medical genetics 2009
Human Monoclonal SMN1 Primary Antibody for IHC, ELISA - ABIN1585251
Zhu, Guo, Yao, Yan, Xue, Hao, Zhou, Zhu, Qin, Lu: Synergy between Kaposi's sarcoma-associated herpesvirus (KSHV) vIL-6 and HIV-1 Nef protein in promotion of angiogenesis and oncogenesis: role of the AKT signaling pathway. in Oncogene 2014
Data show that the coding sequence of survival of motor neuron 2 (SMN2) differs from that of survival motor neuron 1 (SMN1) by a single nucleotide (c.840C>T) at codon 280 in exon 7.
SMN (show SNRPN Antibodies) protein functions in cytoplasmic Sm-core assembly and in the recruitment of the snRNA cap hypermethylase
muscle does not appear to require high levels of SMN (show STMN1 Antibodies) above what is produced by two copies of SMN2
Findings demonstrate that high expression of SMN (show STMN1 Antibodies) in the motor neuron is both necessary and sufficient for proper function of the motor unit. In addition, SMN (show STMN1 Antibodies) high expression in neurons and glia has a major impact on survival.
This study identifies pathways related to the function of Smn (show STMN1 Antibodies) and associated with differential motor unit vulnerability, thus presenting a number of exciting targets for future therapeutic development.
Smn (show STMN1 Antibodies) complex deficiency caused constipation, delayed gastric emptying, slow intestinal transit and reduced colonic motility.
Primary cell culture and two different SMA model mice to demonstrate that reduced levels of Smn (show STMN1 Antibodies) lead to a profound disruption in the expression of myogenic genes.
Results suggest that SMN (show STMN1 Antibodies) plays a role in the maintenance of pluripotent embryonic stem cells and neuronal differentiation in mice.
AAV9-mediated SMN (show STMN1 Antibodies) gene therapy elicits cure for spinal muscular atrophy.
Data show that changes in U12 introns-dependent splicing become apparent after prolonged/extensive survival motor neuron proteins SMN (show STMN1 Antibodies) depletion.
This work both reveals a new autoregulatory pathway governing SMN (show STMN1 Antibodies) expression, and identifies a new mechanism through which SMN (show STMN1 Antibodies) can modulate specific mRNA expression via Gemin5 (show GEMIN5 Antibodies).
SMN (show STMN1 Antibodies) is involved in the axonal translocation of hnRNP R (show HNRNPR Antibodies) and hnRNP R (show HNRNPR Antibodies)-bound RNA/protein complexes.
The results of this study show that, the plasmid containing UTR (show UTS2R Antibodies) elements causes to twice more SMN (show STMN1 Antibodies) gene expression in transfected cells.
The Cajal bodies fail to recruit SMN (show STMN1 Antibodies) and spliceosomal snRNPs, but contain the proteasome activator PA28, a molecular marker associated with the cellular stress response.
PLS3 (show PLS3 Antibodies) is a genuine spinal muscular atrophy protective modifier in SMN1-deleted individuals
Measurements of SMN (show STMN1 Antibodies) and PLS3 (show PLS3 Antibodies) transcript and protein levels in induced pluripotent stem cell-derived motor neurons show limited value as Spinal muscular atrophy biomarkers.
The diverse a-SMN (show STMN1 Antibodies) vs FL-SMN (show STMN1 Antibodies) C-terminus may dictate different protein interactions and complex formation explaining the different localization and role in the neuronal compartment, and the lower expression and stability of a-SMN (show STMN1 Antibodies).
SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control transcriptional termination
Among 43 identified patients with spinal muscular atrophy, 37 (86.0%) showed homozygous deletion of SMN1 exon 7.
Study detected 3 small mutations in 4 patients without homozygous deletion of the SMN1 gene, suggested that about 4% of spinal muscular atrophy patients have subtle mutations and might be considered in laboratory examination
SMN1 Gene Point Mutations in Type I-IV Proximal Spinal Muscular Atrophy Patients with a Single Copy of SMN1
first cloning and identification of the swine SMN1 gene and show that there is significant sequence homology between swine and human SMN (show SNRPN Antibodies) throughout the coding region
This gene is part of a 500 kb inverted duplication on chromosome 5q13. This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions. The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region. The telomeric and centromeric copies of this gene are nearly identical and encode the same protein. However, mutations in this gene, the telomeric copy, are associated with spinal muscular atrophy\; mutations in the centromeric copy do not lead to disease. The centromeric copy may be a modifier of disease caused by mutation in the telomeric copy. The critical sequence difference between the two genes is a single nucleotide in exon 7, which is thought to be an exon splice enhancer. Note that the nine exons of both the telomeric and centromeric copies are designated historically as exon 1, 2a, 2b, and 3-8. It is thought that gene conversion events may involve the two genes, leading to varying copy numbers of each gene. The protein encoded by this gene localizes to both the cytoplasm and the nucleus. Within the nucleus, the protein localizes to subnuclear bodies called gems which are found near coiled bodies containing high concentrations of small ribonucleoproteins (snRNPs). This protein forms heteromeric complexes with proteins such as SIP1 and GEMIN4, and also interacts with several proteins known to be involved in the biogenesis of snRNPs, such as hnRNP U protein and the small nucleolar RNA binding protein. Two transcript variants encoding distinct isoforms have been described.
survival of motor neuron 2, centromeric
, survival motor neuron protein
, ATP-dependent helicase IGHMBP2
, DNA-binding protein SMUBP-2
, antifreeze enhancer-binding protein
, cardiac transcription factor 1
, immunoglobulin S mu binding protein 2
, immunoglobulin mu-binding protein 2
, neuromuscular degeneration
, p110 subunit
, survival of motor neuron protein
, component of gems 1
, survival motor neuron 1 protein
, tudor domain containing 16A
, survival motor neuron 1