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The antibody against RBM15 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 530-780 of human RBM15 (NP_001188474.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IHC-P, ELISA.
The antibody against RBM15 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 530-780 of human RBM15 (NP_001188474.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IHC-P, ELISA.
| Cat.No | ADA-11219A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | RBM15 |
| Target Synonyms | OTT; OTT1; SPEN; RBM15 | Form | Liquid |
| Species Reactivity | Human, Mouse | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.02% sodium azide, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | HepG2, HL-60 | Application | ELISA, WB, IHC-P |
| Immunogen Description | Recombinant fusion protein containing a sequence corresponding to amino acids 530-780 of human RBM15 (NP_001188474.1). | Target Species | Human |
|---|---|---|---|
| Uniprot ID | Q96T37 | Immunogen Sequence |
Uniprot Id
Q96T37
Target Species
Human
Target Name
RBM15
Target Full Name
RNA-binding protein 15
Target Function
RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex. Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist. Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation. Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation. Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen. Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL. May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing. High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing. May be implicated in HOX gene regulation.
Target Involvement
A chromosomal aberration involving RBM15 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with MKL1. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene.
Target Subcellular Location
Nucleus speckle. Nucleus, nucleoplasm. Nucleus envelope. Nucleus membrane; Peripheral membrane protein.
Target Protein Families
RRM Spen family
Target Synonyms
One twenty two protein ; One-twenty two protein 1; OTT; OTT1; Putative RNA-binding protein 15; RBM15; RBM15_HUMAN; RNA binding motif protein 15; RNA-binding motif protein 15
Target Background
Members of the SPEN (Split-end) family of proteins, including RBM15, have repressor function in several signaling pathways and may bind to RNA through interaction with spliceosome components (Hiriart et al., 2005 [PubMed 16129689]).
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