RBM24 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
- 背景知识
Application
| WB, IHC-P, FC, E |
|---|---|
| Primary Accession | Q9BX46 |
| Other Accession | Q7T3I7, Q62176, Q9H0Z9, D3Z4I3, NP_694565.1 |
| Reactivity | Human, Mouse |
| Predicted | Xenopus |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 24776 Da |
| Antigen Region | 4-32 aa |
| Gene ID | 221662 |
|---|---|
| Other Names | RNA-binding protein 24, RNA-binding motif protein 24, RNA-binding region-containing protein 6, RBM24, RNPC6 |
| Target/Specificity | This RBM24 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 4-32 amino acids from the N-terminal region of human RBM24. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 FC~~1:10~50 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | RBM24 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | RBM24 (HGNC:21539) |
|---|---|
| Synonyms | RNPC6 |
| Function | Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation (PubMed:20977548, PubMed:24375645, PubMed:29104163, PubMed:29358667). Plays a major role in pre-mRNA alternative splicing regulation (PubMed:26990106, PubMed:29104163). Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation (PubMed:29104163). Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing (By similarity). Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes (PubMed:26990106). Plays a role in the regulation of mRNA stability (PubMed:20977548, PubMed:24356969, PubMed:24375645, PubMed:29104163). Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities (PubMed:20977548, PubMed:24356969). Involved in myogenic differentiation by regulating MYOG levels (PubMed:20977548). Binds to multiple regions in the mRNA 3'-UTR of TP63 isoform 2, hence inducing its destabilization (PubMed:24375645). Also promotes the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence (PubMed:29104163). Plays a role in the regulation of mRNA translation (PubMed:29358667). Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation (PubMed:29358667). Binds to a huge amount of mRNAs (PubMed:29104163). Required for embryonic heart development, sarcomer and M-band formation in striated muscles (By similarity). Together with RBM20, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity). |
| Cellular Location | Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm {ECO:0000250|UniProtKB:D3Z4I3} |
| Tissue Location | Expressed in fetal and adult heart and skeletal muscles (PubMed:22345307, PubMed:25313962) |
Research Areas
For Research Use Only. Not For Use In Diagnostic Procedures.
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
RBM24 is preferentially expressed in muscle during differentiation in vitro and may regulate myogenic differentiation.
REFERENCES
Miyamoto, S., et al. Genes Cells 14(11):1241-1252(2009)
Lim, J., et al. Cell 125(4):801-814(2006)
Mungall, A.J., et al. Nature 425(6960):805-811(2003)
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