| Overview |
| bs-70627r-100ul |
| Profilin (C-terminal region) Antibody |
| WB |
| The antibody detects a 15 kDa band corresponding to the apparent molecular mass of Profilin-1 in human Jurkat and A431 cells, as well as rat PC12 cells. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Rabbit |
| Profilin synthetic peptide (coupled to carrier protein) that includes amino acids from the C-terminal region of human Profilin-1. |
| Polyclonal |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
| Target |
| P07737 |
| Epididymis Li184a Profilin PFN1 PFN2 |
| Profilins are small actin-binding proteins that have functions in cell motility, cytokinesis, gene transcription, endocytosis and neuronal plasticity. Four profilin isoforms have been identified in mammals. Profilin-1 (PFN1) and profilin-2a (PFN2a) isoforms are highly conserved in structure, but PFN1 is ubiquitously expressed while PFN2a is preferentially enriched in brain. In addition, there are two testis-specific profilins, PFN3 and PFN4, that significantly differ in primary sequence and function compared to PFN1 and PFN2a. Profilin is phosphorylated at both tyrosine and serine residues in vivo. Tyr-129 is phosphorylated in response to VEGF-A stimulation, and this promotes profilin actin binding and polymerization. Tyr-129 phosphorylation may be important for angiogenesis induced by injuries. Ser-138 is phosphorylated by ROCK and dephosphorylated by PP1. This serine phosphorylation inhibits G-actin binding, as well as decreases profilin's aggregation suppressor activity by inhibiting binding to huntingtin. Thus, Tyr-129 phosphorylation may activate while Ser-138 phosphorylation may inhibit profilin activity. |
| Application Dilution |
| WB |
1:300-5000 |
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