Actin
Actin is a ubiquitous globular protein that is one of the most highly-conserved proteins known. It is found in two main states: G-actin is the globular monomeric form, whereas F-actin forms helical polymers. Both G- and F-actin are intrinsically flexible structures.
Actin Inhibitors |
|
|---|---|
| Cat. No. | 产品名称/活性 |
| 3950 | CK 666 |
| Arp2/3 inhibitor; inhibits actin polymerization | |
| 5474 | Cytochalasin B |
| Inhibitor of actin polymerization | |
| 3973 | Latrunculin A |
| Inhibitor of actin assembly and polymerization | |
| 3974 | Latrunculin B |
| Inhibitor of actin polymerization | |
| 4434 | Wiskostatin |
| N-WASP inhibitor; inhibits Arp2/3 activation | |
Other |
|
| Cat. No. | 产品名称/活性 |
| 1233 | Cytochalasin D |
| Disrupts actin filament function | |
| 2792 | Jasplakinolide |
| Stabilizes F-actin; promotes actin polymerization | |
| 3715 | Narciclasine |
| Antiproliferative agent; induces actin polymerization | |
| 4535 | Phalloidin |
| Promotes actin polymerization | |
| 5782 | Phalloidin-FITC |
| Green fluorescent cytoskeleton stain | |
| 5783 | Phalloidin-TRITC |
| Red-orange fluorescent cytoskeleton stain | |
Actin is a ubiquitous globular protein that is one of the most highly-conserved proteins known. It is found in two main states: G-actin is the globular monomeric form, whereas F-actin forms helical polymers. Both G- and F-actin are intrinsically flexible structures - a feature vital in actin's role as a dynamic filament network.
Actin has four major functions. Firstly, F-actin polymers form microfilaments - polar intracellular 'tracks' for kinesin motor proteins, allowing the transport of vesicles, organelles and other cargo. Actin is a component of the cytoskeleton and links to α-actinin, E-cadherin and β-catenin at adherens junctions. This gives mechanical support to cells and attaches them to each other and the extracellular matrix. In muscle cells, actin-rich thin filaments associate with myosin-rich thick filaments to form actomyosin myofibrils. Using energy from the hydrolysis of ATP, myofibrils undergo cyclic shortening through actin-myosin head interactions, which represents the mechanics of muscle contraction. Finally, actin has a role in cell motility through polymerization and depolymerization of fibrils.
Actin Gene Data
| Gene | Species | Gene Symbol | Gene Accession No. | Protein Accession No. |
|---|---|---|---|---|
| α1 actin | Human | ACTA1 | NM_001100 | P68133 |
| Mouse | Acta1 | NM_009606 | P68134 | |
| Rat | Acta1 | NM_019212 | NP_062085 | |
| α2 actin | Human | ACTA2 | NM_001613 | P62736 |
| Mouse | Acta2 | NM_007392 | P62737 | |
| Rat | Acta2 | NM_031004 | P62738 | |
| β actin | Human | ACTB | NM_001101 | Q96HG5 |
| Mouse | Actb | NM_007393 | P60710 | |
| Rat | Actb | NM_031144 | P60711 | |
| γ1 actin | Human | ACTG1 | NM_001614 | P63261 |
| Mouse | Actg1 | NM_009609 | P63260 | |
| Rat | Actg1 | NM_001127449 | P63259 | |
| γ2 actin | Human | ACTG2 | NM_001615 | P63267 |
| Mouse | Actg2 | NM_009610 | P63268 | |
| Rat | Actg2 | NM_012893 | P63269 |