Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
Phospho-Ser503 Kv3.1, Voltage-Gated, Potassium Channel Antibody
Affinity purified rabbit polyclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC |
|---|---|
| Primary Accession | P25122 |
| Reactivity | Mouse, Rat |
| Host | Rabbit |
| Clonality | polyclonal |
| Calculated MW | 100 KDa |
| Gene ID | 25327 |
|---|---|
| Gene Name | KCNC1 |
| Other Names | Potassium voltage-gated channel subfamily C member 1, NGK2, RAW2, Voltage-gated potassium channel subunit Kv31, Voltage-gated potassium channel subunit Kv4, Kcnc1 |
| Target/Specificity | Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser503 conjugated to KLH. |
| Dilution | IHC~~ 1:1000 |
| Format | Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns. |
| Antibody Specificity | Specific for the ~100k Kv3.1 voltage-gated potassium channel proteinphosphorylated at Ser503. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Phospho-Ser503 Kv3.1, Voltage-Gated, Potassium Channel Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
Voltage-gated K+ channels are important determinants of neuronal membrane excitability. Moreover, differences in K+ channel expression patterns and densities contribute to the variations in action potential waveforms and repetitive firing patterns evident in different neuronal cell types (Maletic-Savatic et al., 1995; Pongs, 1999; Blaine and Ribera, 1998; Burger and Ribera, 1996). The Kv3.1 potassium channel is expressed at high levels in neurons that characteristically fire rapid trains of action potentials (Gan et al., 1999).
References
Blaine JT, Ribera AB (1998) Heteromultimeric potassium channels formed by members of the Kv2 subfamily. J
Neurosci 18:9585-9593.
Burger C, Ribera AB (1996) Xenopus spinal neurons express Kv2 potassium channel transcripts during embryonic
development. J Neurosci 16:1412-1421.
Gan L, Hahn SJ, Kaczmarek LK (1999) Cell type-specific expression of the Kv3.1 gene is mediated by a negative
element in the 5' untranslated region of the Kv3.1 promoter. J Neurochem 73:1350-1362.
Maletic-Savatic M, Lenn NJ, Trimmer JS (1995) Differential spatiotemporal expression of K+ channel polypeptides in
rat hippocampal neurons developing in situ and in vitro. J Neurosci 15:3840-3851.
Pongs O (1999) Voltage-gated potassium channels: from hyperexcitability to excitement. FEBS Lett 452:31-35.
von Hehn CA, Bhattacharjee A, Kaczmarek LK (2004) Loss of Kv3.1 tonotopicity and alterations in cAMP response
element-binding protein signaling in central auditory neurons of hearing impaired mice. J Neurosci 24:1936-1940.
Ping Song and Leonard K. Kaczmarek (2006) Modulation of Kv3.1b Potassium Channel Phosphorylation in Auditory
Neurons by Conventional and Novel Protein Kinase C IsozymesJ. Biol. Chem., Jun
2006; 281: 15582 - 15591
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
