Combimicin B1
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| Category | Antibiotics |
| Catalog number | BBF-01045 |
| CAS | 72265-93-1 |
| Molecular Weight | 493.59 |
| Molecular Formula | C21H43N5O8 |
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Description
It is produced by the strain of Micromonospora sp. K-6993, K-6993-Y-41, NRRL 2958-N-6. It's a kanamycin homolog.
Specification
| IUPAC Name | 6-((4,6-diamino-3-((3-amino-6-((methylamino)methyl)tetrahydro-2H-pyran-2-yl)oxy)-2-hydroxycyclohexyl)oxy)-2-(hydroxymethyl)-3-methyl-4-(methylamino)tetrahydro-2H-pyran-3,5-diol |
Properties
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria |
| Melting Point | 108-111 °C |
| Solubility | Soluble in Water |
Reference Reading
1. B1 siRNA Increases de novo DNA Methylation of B1 Elements and Promotes Wound Healing in Diabetic Rats
Sakawdaurn Yasom, Wilunplus Khumsri, Papatson Boonsongserm, Nakarin Kitkumthorn, Preecha Ruangvejvorachai, Apasee Sooksamran, Rujira Wanotayan, Apiwat Mutirangura Front Cell Dev Biol. 2022 Jan 19;9:802024. doi: 10.3389/fcell.2021.802024. eCollection 2021.
Alu (B1 in rodents) hypomethylation, commonly found in diabetes mellitus patients, increases DNA damage and, consequently, delays the healing process. Alu siRNA increases Alu methylation, reduces DNA damage, and promotes cell proliferation. Aim: To explore whether B1 siRNA treatment restores B1 hypomethylation, resulting in a reduction in DNA damage and acceleration of the healing process in diabetic rat wounds. Methods: We generated splinted-excisional wounds in a streptozotocin (STZ)-induced type I diabetic rat model and treated the wounds with B1 siRNA/Ca-P nanoparticles to generate de novo DNA methylation in B1 intersperse elements. After treatment, we investigated B1 methylation levels, wound closure rate, wound histopathological structure, and DNA damage markers in diabetic wounds compared to nondiabetic wounds. Results: We reported that STZ-induced diabetic rat wounds exhibited B1 hypomethylation, wound repair defects, anatomical feature defects, and greater DNA damage compared to normal rats. We also determined that B1 siRNA treatment by Ca-P nanoparticle delivery restored a decrease in B1 methylation levels, remedied delayed wound healing, and improved the histological appearance of the wounds by reducing DNA damage. Conclusion: B1 hypomethylation is inducible in an STZ-induced type I diabetes rat model. Restoration of B1 hypomethylation using B1 siRNA leads to increased genome stability and improved wound repair in diabetes. Thus, B1 siRNA intervention may be a promising strategy for reprogramming DNA methylation to treat or prevent DNA damage-related diseases.
2. Heterogeneous nuclear ribonucleoprotein hnRNPA2/B1 regulates the abundance of the copper-transporter ATP7A in an isoform-dependent manner
Courtney J McCann, Nesrin M Hasan, Teresita Padilla-Benavides, Shubhrajit Roy, Svetlana Lutsenko Front Mol Biosci. 2022 Dec 5;9:1067490. doi: 10.3389/fmolb.2022.1067490. eCollection 2022.
Copper (Cu) is an essential micronutrient with a critical role in mammalian growth and development. Imbalance of Cu causes severe diseases in humans; therefore, cellular Cu levels are tightly regulated. Major Cu-transport proteins and their cellular behavior have been characterized in detail, whereas their regulation at the mRNA level and associated factors are not well-understood. We show that the heterogeneous nuclear ribonucleoprotein hnRNPA2/B1 regulates Cu homeostasis by modulating the abundance of Cu(I)-transporter ATP7A. Downregulation of hnRNPA2/B1 in HeLa cells increases the ATP7A mRNA and protein levels and significantly decreases cellular Cu; this regulation involves the 3' UTR of ATP7A transcript. Downregulation of B1 and B1b isoforms of hnRNPA2/B1 is sufficient to elevate ATP7A, whereas overexpression of either hnRNPA2 or hnRNPB1 isoforms decreases the ATP7A mRNA levels. Concurrent decrease in hnRNPA2/B1, increase in ATP7A, and a decrease in Cu levels was observed in neuroblastoma SH-SY5Y cells during retinoic acid-induced differentiation; this effect was reversed by overexpression of B1/B1b isoforms. We conclude that hnRNPA2/B1 is a new isoform-specific negative regulator of ATP7A abundance.
3. PTBP1 promotes IRES-mediated translation of cyclin B1 in cancer
Xinyi Fan, Zitong Zhao, Liying Ma, Xuanlin Huang, Qimin Zhan, Yongmei Song Acta Biochim Biophys Sin (Shanghai). 2022 May 25;54(5):696-707. doi: 10.3724/abbs.2022046. Online ahead of print.
Cyclin B1 is an essential cyclin-dependent protein that involves in the G2/M transition. Multiple studies report that cyclin B1 is upregulated in cancers and promotes cancer progression. However, the mechanism of cyclin B1 upregulation remains unclear. Here we report that the 5'UTR of cyclin B1 mRNA contains an internal ribosome entry site (IRES) by using a bicistronic fluorescent reporter. We show that IRES can initiate the translation of cyclin B1, and the IRES-mediated translation is further activated under cell stress. Interacting trans-acting factors (ITAFs) are required by most IRES to initiate the translation. We find that PTBP1 promotes the IRES-mediated translation of cyclin B1 by binding to the 5'UTR of cyclin B1. On top of that, PTBP1 promotes the malignancy of ESCC cells. Our data suggest that the IRES-mediated translation of cyclin B1 plays an essential role in the cyclin B1 upregulation in cancers.
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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 ╳
