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Anti-Rabphilin 3A (Ser234) Antibody
Our Anti-Rabphilin 3A (Ser234) rabbit polyclonal phosphospecific primary antibody from PhosphoSoluti
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | P47709 |
| Reactivity | Bovine |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 75832 Da |
| Gene ID | 171039 |
|---|---|
| Other Names | Exophilin 1 antibody, Exophilin-1 antibody, Exophilin1 antibody, KIAA0985 antibody, Rabphilin 3A homolog antibody, Rabphilin-3A antibody, Rabphilin3A antibody, RP3A antibody, RP3A_HUMAN antibody, Rph 3a antibody, Rph3a antibody |
| Target/Specificity | Rabphilin-3A is a peripheral membrane protein that binds Ca2+ and phospholipids and is attached to synaptic vesicle membranes (Geppert et al., 1994; Li et al., 1994). The expression of rabphilin 3A is reduced in an animal model of Huntington’s disease (Smith et al., 2005). Rabphilin can be phosphorylated at Ser-234 by both CAM kinase II and PKA and this phosphorylation has been suggested to regulate neuronal activity during development in a synapse-specific manner (Fykse et al., 1995; Foletti and Scheller, 2001). |
| Dilution | WB~~1:1000 |
| Format | Antigen Affinity Purified from Pooled Serum |
| 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 | Anti-Rabphilin 3A (Ser234) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
Rabphilin-3A is a peripheral membrane protein that binds Ca2+ and phospholipids and is attached to synaptic vesicle membranes (Geppert et al., 1994; Li et al., 1994). The expression of rabphilin 3A is reduced in an animal model of Huntington’s disease (Smith et al., 2005). Rabphilin can be phosphorylated at Ser-234 by both CAM kinase II and PKA and this phosphorylation has been suggested to regulate neuronal activity during development in a synapse-specific manner (Fykse et al., 1995; Foletti and Scheller, 2001).
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