Anti-Recombinant-TPM1 antibody [RM1M09] (STJA0023696)
SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
General Information
| Short Description | Rabbit monoclonal anti-Recombinant-Tropomyosin Alpha-1 Chain for use in FC, IF, IHC, IP and WB in Human, Mouse and Rat samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | FC/IF/IHC/IP/WB |
| Host | Rabbit |
| Reactivity | Human/Mouse/Rat |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Monoclonal |
| Clone ID | RM1M09 |
| Isotype | IgG |
| Conjugation | Unconjugated |
| Purification | Protein A/G purified from cell culture supernatant |
| Dilution Range | FCM: 1:20-1:100 |
| Formulation | 0.01M PBS |
| Storage Instruction | Suitable for storage at +4°C between 1-2 weeks. For longer term store at-20°C for up to 12 months. |
Target Information
| Gene Symbol | TPM1 |
| Gene ID | 7168 |
| Uniprot ID | TPM1_HUMAN |
Additional Info
| Post Translational Modifications | Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells. |
| Function | Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. |
| Protein Name | Tropomyosin Alpha-1 ChainAlpha-TropomyosinTropomyosin-1 |
| Database Links | Reactome: R-HSA-390522Reactome: R-HSA-445355 |
| Cellular Localisation | CytoplasmCytoskeletonAssociates With F-Actin Stress Fibers |
| Alternative Antibody Names | Anti-Tropomyosin Alpha-1 Chain antibodyAnti-Alpha-Tropomyosin antibodyAnti-Tropomyosin-1 antibodyAnti-TPM1 antibodyAnti-C15orf13 antibodyAnti-TMSA antibody |
Information sourced from Uniprot.org