Mouse Clk4 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | O35493 |
Other Accession | NP_031740.1 |
Reactivity | Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 57345 Da |
Antigen Region | 49-77 aa |
Gene ID | 12750 |
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Other Names | Dual specificity protein kinase CLK4, CDC-like kinase 4, Clk4 |
Target/Specificity | This Mouse Clk4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 49-77 amino acids from the N-terminal region of mouse Clk4. |
Dilution | WB~~1:1000 |
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 | Mouse Clk4 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | Clk4 |
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Function | Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine- rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. |
Cellular Location | Nucleus. |
Tissue Location | Expressed in the hippocampus, the cerebellum and the olfactory bulb. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Phosphorylates serine-and arginine-rich (SR) proteins of the spliceosomal complex may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates serines, threonines and tyrosines. Required for the regulation of alternative splicing of MAPT/TAU.
References
Katsu, R., et al. J. Biol. Chem. 277(46):44220-44228(2002)
Hartmann, A.M., et al. Mol. Cell. Neurosci. 18(1):80-90(2001)
Watkins-Chow, D.E., et al. Genomics 45(1):147-157(1997)
Nayler, O., et al. Biochem. J. 326 (PT 3), 693-700 (1997) :
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