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HNRNPM belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). Additionally we are shipping Heterogeneous Nuclear Ribonucleoprotein M Kits (17) and Heterogeneous Nuclear Ribonucleoprotein M Proteins (6) and many more products for this protein.
Showing 10 out of 85 products:
Cow (Bovine) Monoclonal HNRNPM Primary Antibody for ICC, IHC (fro) - ABIN152355
Kafasla, Patrinou-Georgoula, Guialis: The 72/74-kDa polypeptides of the 70-110 S large heterogeneous nuclear ribonucleoprotein complex (LH-nRNP) represent a discrete subset of the hnRNP M protein family. in The Biochemical journal 2001
Show all 6 Pubmed References
Cow (Bovine) Monoclonal HNRNPM Primary Antibody for ICC, IF - ABIN152356
Vautier, Chesné, Cunha, Calado, Renard, Carmo-Fonseca: Transcription-dependent nucleocytoplasmic distribution of hnRNP A1 protein in early mouse embryos. in Journal of cell science 2001
Show all 2 Pubmed References
Cow (Bovine) Polyclonal HNRNPM Primary Antibody for WB - ABIN2778962
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... in Molecular systems biology 2007
Show all 2 Pubmed References
Human Monoclonal HNRNPM Primary Antibody for IF, IHC (p) - ABIN518184
Jeon, Jeong, Baek, Koo, Park, Yang, Yu, Kim, Pak: Network clustering revealed the systemic alterations of mitochondrial protein expression. in PLoS computational biology 2011
Human Polyclonal HNRNPM Primary Antibody for ELISA, WB - ABIN561915
Venables, Koh, Froehlich, Lapointe, Couture, Inkel, Bramard, Paquet, Watier, Durand, Lucier, Gervais-Bird, Tremblay, Prinos, Klinck, Elela, Chabot: Multiple and specific mRNA processing targets for the major human hnRNP proteins. in Molecular and cellular biology 2008
suggesting that Rump and Lost are part of a core localization complex that promotes utilization of the late localization pathway by multiple mRNAs in parallel
Data show that depletion of Hrp59 by RNA interference reduces the levels of Rrp4 at transcription sites, which suggests that Hrp59 is needed for the exosome to stably interact with nascent pre-mRNPs.
Hrp59 is required for the expression of target mRNAs. Hrp59 binds preferentially to exonic splicing enhancers and our results provide new insights into the role of hnRNP M in splicing regulation.
the ability of HRP59 to regulate the alternative splicing of its own pre-mRNA serves in a negative feedback loop that controls the levels of the HRP59 protein and maintains the homeostasis of the splicing environment.
Rumpelstiltskin (rump) regulates anterior-posterior axis patterning by functioning as a direct-acting nanos mRNA localization factor.
Overexpression of hnRNPM promotes breast cancer aggressiveness by regulating the level of CD44s and indicates a poor prognosis.
Data suggest that both heterogeneous nuclear ribonucleoprotein (show PCBP2 Antibodies) type M (HNRPM) and solute carrier (show SERTAD2 Antibodies) 1A5 (SLC1A5 (show SLC1A5 Antibodies)) have role in the pathogenesis of ovarian cancer.
p54nrb and hnRNPM knockdown silences the FGF1 promoter-dependent accumulation of mRNA during myoblast differentiation.
Results suggest that glyceraldehyde-modified hnRNPM alters gene expression in nonalcoholic fatty liver disease.
The authors propose that cleavage of and subverting the function of hnRNPM by 3C protease is a general strategy utilized by picornaviruses to facilitate viral infection.
our data suggest that TAF15 (show TAF15 Antibodies) and TLS/FUS (show FUS Antibodies) operate within similar but not identical hnRNP M-TET protein complexes to influence the transcriptional or post-transcriptional output of a particular cell type.
findings demonstrate a novel molecular mechanism through which tumor metastasis is endowed by the hnRNPM-mediated splicing program.
Our results provide a clue that hnRNP M is a potential therapeutic target for Spinal muscular atrophy
The present data demonstrate that the upregulation of HnRNP M is involved in human colorectal epithelial carcinogenesis and may serve as a carcinoma biomarker for colorectal cancer.
Mechanistic control of carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM1 (show CEACAM1 Antibodies)) splice isoforms by the heterogeneous nuclear ribonuclear proteins hnRNP L (show HNRNPL Antibodies), hnRNP A1 (show HNRNPA1 Antibodies), and hnRNP M.
identify Nova-1 (show NOVA1 Antibodies) and hnRNP M as D2R (show DRD2 Antibodies) pre-mRNA-binding proteins and show their antagonistic role in the alternative splicing of D2R (show DRD2 Antibodies) pre-mRNA.
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has three repeats of quasi-RRM domains that bind to RNAs. This protein also constitutes a monomer of the N-acetylglucosamine-specific receptor which is postulated to trigger selective recycling of immature GlcNAc-bearing thyroglobulin molecules. Alternative splicing results in multiple transcript variants.
heterogeneous nuclear ribonucleoprotein M
, Heterogeneous nuclear ribonucleoprotein M
, heterogeneous nuclear ribonucleoprotein M-like
, CEA receptor
, N-acetylglucosamine receptor 1
, heterogenous nuclear ribonucleoprotein M4
, hnRNA-binding protein M4
, hnRNP M
, M4 protein