RBM15 Antibody [L5G12] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Lane 1: 22Rv1, Lane 2: NIH/3T3, Lane 3: H-4-II-E, Lane 4: COS-7

Usage Information

Dilution
WB1:1000 IP1:50

Application
WB, IP

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
110 kDa

Datasheet & SDS

Biological Description

Specificity
RBM15 Antibody [L5G12] detects endogenous levels of total RBM15 protein.

Clone
L5G12

Synonym(s)
RNA-binding motif protein 15; One-twenty two protein; RBM15; OTT; OTT1

Background
RBM15 belongs to the SPEN family of RNA-binding proteins characterized by multiple RNA recognition motifs and a conserved SPOC domain that orchestrates interactions with splicing and methylation machinery. It features an N-terminal region with RRM domains for sequence-specific pre-mRNA binding alongside a C-terminal SPOC that engages phosphorylated WTAP and RNA polymerase II CTD to anchor regulatory complexes at nascent transcripts. RBM15 recruits the WTAP-METTL3-METTL14 m6A methyltransferase complex to intronic and 3' UTR sites, installing N6-methyladenosine marks that direct alternative splicing outcomes and mRNA export through NXF1-mediated nuclear transport. Interaction with the U2 snRNP-associated SF3B1 splicing factor targets weak branch point regions, facilitating cassette exon inclusion or skipping in transcripts encoding hematopoietic regulators like GATA1, RUNX1, TAL1, and c-MPL to calibrate lineage commitment during megakaryopoiesis and myeloid differentiation. PRMT1-mediated arginine dimethylation at R578 triggers E3 ligase CNOT4 recognition, promoting K48-linked ubiquitination and proteasomal degradation that fine-tunes RBM15 steady-state levels in response to thrombopoietin signaling. RBM15 balances proliferation versus terminal maturation by modulating Mpl isoform splicing, where full-length receptors amplify self-renewal signals while truncated dominant-negative forms restrain expansion. Elevated RBM15 drives acute megakaryoblastic leukemia through fusion with MKL1, sustaining oncogenic splicing networks that evade differentiation blocks.

Background

RBM15 belongs to the SPEN family of RNA-binding proteins characterized by multiple RNA recognition motifs and a conserved SPOC domain that orchestrates interactions with splicing and methylation machinery. It features an N-terminal region with RRM domains for sequence-specific pre-mRNA binding alongside a C-terminal SPOC that engages phosphorylated WTAP and RNA polymerase II CTD to anchor regulatory complexes at nascent transcripts. RBM15 recruits the WTAP-METTL3-METTL14 m6A methyltransferase complex to intronic and 3' UTR sites, installing N6-methyladenosine marks that direct alternative splicing outcomes and mRNA export through NXF1-mediated nuclear transport. Interaction with the U2 snRNP-associated SF3B1 splicing factor targets weak branch point regions, facilitating cassette exon inclusion or skipping in transcripts encoding hematopoietic regulators like GATA1, RUNX1, TAL1, and c-MPL to calibrate lineage commitment during megakaryopoiesis and myeloid differentiation. PRMT1-mediated arginine dimethylation at R578 triggers E3 ligase CNOT4 recognition, promoting K48-linked ubiquitination and proteasomal degradation that fine-tunes RBM15 steady-state levels in response to thrombopoietin signaling. RBM15 balances proliferation versus terminal maturation by modulating Mpl isoform splicing, where full-length receptors amplify self-renewal signals while truncated dominant-negative forms restrain expansion. Elevated RBM15 drives acute megakaryoblastic leukemia through fusion with MKL1, sustaining oncogenic splicing networks that evade differentiation blocks.

References
https://www.sciencedirect.com/science/article/pii/S0006497118511009 https://pubmed.ncbi.nlm.nih.gov/26575292/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%