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The protein encoded by SNRPN is one polypeptide of a small nuclear ribonucleoprotein complex and belongs to the snRNP SMB/SMN family. Additionally we are shipping SNRPN Proteins (8) and many more products for this protein.
Showing 10 out of 70 products:
Human Monoclonal SNRPN Primary Antibody for ICC, IF - ABIN151435
Giesemann, Rathke-Hartlieb, Rothkegel, Bartsch, Buchmeier, Jockusch, Jockusch: A role for polyproline motifs in the spinal muscular atrophy protein SMN. Profilins bind to and colocalize with smn in nuclear gems. in The Journal of biological chemistry 2000
Show all 19 references for 151435
Dog (Canine) Monoclonal SNRPN Primary Antibody for BI, IHC (f) - ABIN968085
Cifuentes-Diaz, Frugier, Tiziano, Lacène, Roblot, Joshi, Moreau, Melki: Deletion of murine SMN exon 7 directed to skeletal muscle leads to severe muscular dystrophy. in The Journal of cell biology 2001
Show all 5 references for 968085
Cow (Bovine) Polyclonal SNRPN Primary Antibody for WB - ABIN610748
Buschmann, Lerner, Lee, Ronai: The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9. in The Journal of biological chemistry 2001
Show all 3 references for 610748
Human Polyclonal SNRPN Primary Antibody for ELISA, WB - ABIN252925
Setola, Terao, Locatelli, Bassanini, Garattini, Battaglia: Axonal-SMN (a-SMN), a protein isoform of the survival motor neuron gene, is specifically involved in axonogenesis. in Proceedings of the National Academy of Sciences of the United States of America 2007
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Human Polyclonal SNRPN Primary Antibody for IHC, IHC (p) - ABIN4354968
Jing, Zhao, Wang, Zhao, Liang, Wang, Ma: Effect of small nuclear ribonucleoprotein-associated polypeptide N on the proliferation of medulloblastoma cells. in Molecular medicine reports 2015
Human Polyclonal SNRPN Primary Antibody for IHC (p), WB - ABIN658453
Kuslich, Kobori, Mohapatra, Gregorio-King, Donlon: Prader-Willi syndrome is caused by disruption of the SNRPN gene. in American journal of human genetics 1999
The androgenetic patterns of H19 (show NCKAP1 Antibodies), Snrpn, and Mest (show MEST Antibodies) were maintained even after differentiation of germline-derived pluripotent stem cells(gPS (show NBEAL2 Antibodies)) into neural stem cells(NSC), whereas the fully unmethylated status of Ndn (show NDN Antibodies) in SSCs was altered to somatic patterns in gPS (show NBEAL2 Antibodies) cells and gPS (show NBEAL2 Antibodies)-NSCs.
These data indicate that oocytes undergo time-dependent demethylation of Snrpn differentially methylated regions during the process of postovulatory aging.
Oocytes vitrification could lead to the loss of DNA methylation (show HELLS Antibodies) of imprinted genes (H19 (show NCKAP1 Antibodies), Peg3 (show PEG3 Antibodies), and Snrpn) in mouse blastocysts, which is mainly caused by the reductions of DNMTs after vitrification of oocytes.
These results support a model in which transcription from the Snrpn upstream exons directs the maternal imprint at the PWS-IC
Snrpn gene is imprinted, with monoallelic expression from the paternal allele in brain and heart.
the ATG-to-AAG (show C16orf35 Antibodies) mutation causes a 15-fold or more increase in translation of the downstream ORF in two fusion constructs, and it is likely that similar translational control affects the normal Snurf-Snrpn (show SNURF Antibodies) transcript as well
The tissue-specific methylation of the mouse conserved activator sequence and its methylation-sensitive enhancer activity may control expression of imprinting center transcripts, establishing and/or maintaining imprinting in the Snrpn locus.
Mouse model for Prader-Willi syndrome. Deletion of Snrpn gene and putative imprinting-centre is associated with absent expression of the imprinted genes Zfp127, Ndn a (show NDN Antibodies)nd Ipw, and phenotypes similar to those found in Prader-Willi infants.
we have confirmed that SNRPN methylation increases with age, which raises further questions regarding the role of SNRPN expression during the aging process.
the cases with partial loss of methylation in KCNQ1OT1 and SNRPN present clinical features different to those associated with the corresponding imprinting syndromes
Knockdown of SNRPN was demonstrated to significantly inhibit medulloblastoma cell growth and induce G2/M phase arrest in vitro.
indicate that SmN (show STMN1 Antibodies) expression reduces the level of mature U2 snRNP (show LSM2 Antibodies), leading to alternative splicing
The methylation patterns of the promoters of MTHFR (show MTHFR Antibodies) and SNRPN are associated with changes in sperm motility and morphology, which could lead to male infertility.
Human amniotic fluid mesenchymal stem cells contain a unique epigenetic signature during in vitro cell culture. H19 (show NCKAP1 Antibodies) and KCNQ1OT1 possessed a substantial degree of hypermethylation status, and variable DNA methylation (show HELLS Antibodies) patterns of SNRPN was observed.
In the skeletal muscle of neonate pigs, both NECD (show NDN Antibodies) and SNRPN were maternally imprinted, while UBE3A (show ube3a Antibodies) was not imprinted.
genetic association studies using 1,000 white subjects from Midwestern United States: Three copy number variations (CNV) in PWCR (show NDN Antibodies) are associated with body fat mass, with a higher copy number (CN) associated with an increase of in body fat mass.
Variable methylation of the imprinted gene, SNRPN, supports a relationship between intracranial germ cell tumours and neural stem cells.
SNRPN gene is imprinted, with monoallelic expression from the paternal allele in fetal brain and heart, and in adult brain.
SNRPN methylation profiles previously observed in mouse and human studies are also conserved in cattle
Results suggest that artificial reproductive techniques, such as prolonged in vitro culture and SCNT, lead to abnormal reprogramming of imprinting of SNRPN gene by altering methylation levels at this locus.
The protein encoded by this gene is one polypeptide of a small nuclear ribonucleoprotein complex and belongs to the snRNP SMB/SMN family. The protein plays a role in pre-mRNA processing, possibly tissue-specific alternative splicing events. Although individual snRNPs are believed to recognize specific nucleic acid sequences through RNA-RNA base pairing, the specific role of this family member is unknown. The protein arises from a bicistronic transcript that also encodes a protein identified as the SNRPN upstream reading frame (SNURF). Multiple transcription initiation sites have been identified and extensive alternative splicing occurs in the 5' untranslated region. Additional splice variants have been described but sequences for the complete transcripts have not been determined. The 5' UTR of this gene has been identified as an imprinting center. Alternative splicing or deletion caused by a translocation event in this paternally-expressed region is responsible for Angelman syndrome or Prader-Willi syndrome due to parental imprint switch failure.
sm protein D
, sm protein N
, small nuclear ribonucleoprotein-associated protein N
, tissue-specific-splicing protein
, SM protein N
, tissue-specific splicing protein
, FE294 gene for snRNP-associated polypeptide N
, FE294 psi pseudogene
, small nuclear ribonucleoparticle-associated protein (snRNP) mRNA clone Sm51
, small nuclear ribonucleoparticle-associated protein (snRNP) mRNA, clone Sm51
, small nuclear ribonucleoprotein N