Thioactin
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Antibiotics |
| Catalog number | BBF-02693 |
| CAS | |
| Molecular Weight | 1057.12 |
| Molecular Formula | C43H40N14O11S4 |
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Description
Thioactin is produced by the strain of Str. sp. DP94. The minimum inducing concentration of X to the promoter TIP-1 was 40 ng/mL.
Specification
| IUPAC Name | N-(3-amino-3-oxoprop-1-en-2-yl)-14-(1-hydroxyethyl)-31-methyl-38,41-dimethylidene-17-(methylsulfanylmethyl)-12,15,22,29,36,39-hexaoxo-19,43-dioxa-9,26,33-trithia-3,13,16,23,30,37,40,45,46,47,48,49-dodecazaheptacyclo[40.2.1.18,11.118,21.125,28.132,35.02,7]nonatetraconta-1(44),2(7),3,5,8(49),10,18(48),20,25(47),27,32(46),34,42(45)-tridecaene-4-carboxamide |
| Canonical SMILES | CC1C2=NC(=CS2)C(=O)NC(=C)C(=O)NC(=C)C3=NC(=CO3)C4=C(C=CC(=N4)C(=O)NC(=C)C(=O)N)C5=NC(=CS5)C(=O)NC(C(=O)NC(C6=NC(=CO6)C(=O)NCC7=NC(=CS7)C(=O)N1)CSC)C(C)O |
| InChI | InChI=1S/C43H40N14O11S4/c1-16(32(44)59)46-35(62)22-8-7-21-31(51-22)23-10-67-40(53-23)18(3)48-33(60)17(2)47-37(64)26-14-71-42(55-26)19(4)49-36(63)25-13-70-29(50-25)9-45-34(61)24-11-68-41(54-24)28(12-69-6)52-39(66)30(20(5)58)57-38(65)27-15-72-43(21)56-27/h7-8,10-11,13-15,19-20,28,30,58H,1-3,9,12H2,4-6H3,(H2,44,59)(H,45,61)(H,46,62)(H,47,64)(H,48,60)(H,49,63)(H,52,66)(H,57,65) |
| InChI Key | OIADYYNTHJZNLB-UHFFFAOYSA-N |
Properties
| Appearance | White Powder |
| Melting Point | 250-255°C |
Reference Reading
1. Tools of the trade: studying actin in zebrafish
Clyde Savio Pinto, Masanori Mishima, Karuna Sampath Histochem Cell Biol. 2020 Nov;154(5):481-493. doi: 10.1007/s00418-020-01932-3. Epub 2020 Oct 23.
Actin is a conserved cytoskeletal protein with essential functions. Here, we review the state-of-the-art reagents, tools and methods used to probe actin biology and functions in zebrafish embryo and larvae. We also discuss specific cell types and tissues where the study of actin in zebrafish has provided new insights into its functions.
2. The dynamic instability of actin filament barbed ends
Guillaume Romet-Lemonne, Antoine Jégou J Cell Biol. 2021 Apr 5;220(4):e202102020. doi: 10.1083/jcb.202102020.
The turnover of actin filament networks in cells has long been considered to reflect the treadmilling behavior of pure actin filaments in vitro, where only the pointed ends depolymerize. Newly discovered molecular mechanisms challenge this notion, as they provide evidence of situations in which growing and depolymerizing barbed ends coexist.
3. Implications of the Actin Cytoskeleton on the Multi-Step Process of [ PSI+] Prion Formation
Jane E Dorweiler, Douglas R Lyke, Nathan P Lemoine, Samantha Guereca, Hannah E Buchholz, Emily R Legan, Claire M Radtke, Anita L Manogaran Viruses. 2022 Jul 21;14(7):1581. doi: 10.3390/v14071581.
Yeast prions are self-perpetuating misfolded proteins that are infectious. In yeast, [PSI+] is the prion form of the Sup35 protein. While the study of [PSI+] has revealed important cellular mechanisms that contribute to prion propagation, the underlying cellular factors that influence prion formation are not well understood. Prion formation has been described as a multi-step process involving both the initial nucleation and growth of aggregates, followed by the subsequent transmission of prion particles to daughter cells. Prior evidence suggests that actin plays a role in this multi-step process, but actin's precise role is unclear. Here, we investigate how actin influences the cell's ability to manage newly formed visible aggregates and how actin influences the transmission of newly formed aggregates to future generations. At early steps, using 3D time-lapse microscopy, several actin mutants, and Markov modeling, we find that the movement of newly formed aggregates is random and actin independent. At later steps, our prion induction studies provide evidence that the transmission of newly formed prion particles to daughter cells is limited by the actin cytoskeletal network. We suspect that this limitation is because actin is used to possibly retain prion particles in the mother cell.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
