LL-BM-781 α1

LL-BM-781 α1

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Category Antibiotics
Catalog number BBF-03621
CAS 72380-11-1
Molecular Weight 982.09
Molecular Formula C39H75N13O16

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Description

It is originally isolated from Nocardia sp. BM 782Ce82 (NRRL 11239). LL-BM-781 α1 has anti-mycobacterium, gram-positive and negative activities.

Specification

Synonyms Antibiotic LL-BM-781 α1

Properties

Appearance White Powder
Antibiotic Activity Spectrum Gram-positive bacteria; Gram-negative bacteria; mycobacteria
Solubility Soluble in Water

Reference Reading

1. Bridging the myoplasmic gap II: more recent advances in skeletal muscle excitation-contraction coupling
Roger A Bannister J Exp Biol. 2016 Jan;219(Pt 2):175-82. doi: 10.1242/jeb.124123.
In skeletal muscle, excitation-contraction (EC) coupling relies on the transmission of an intermolecular signal from the voltage-sensing regions of the L-type Ca(2+) channel (Ca(V)1.1) in the plasma membrane to the channel pore of the type 1 ryanodine receptor (RyR1) nearly 10 nm away in the membrane of the sarcoplasmic reticulum (SR). Even though the roles of Ca(V)1.1 and RyR1 as voltage sensor and SR Ca(2+) release channel, respectively, have been established for nearly 25 years, the mechanism underlying communication between these two channels remains undefined. In the course of this article, I will review current viewpoints on this topic with particular emphasis on recent studies.
2. Engineering the serpin α1 -antitrypsin: A diversity of goals and techniques
Benjamin M Scott, William P Sheffield Protein Sci. 2020 Apr;29(4):856-871. doi: 10.1002/pro.3794. Epub 2019 Dec 9.
α1 -Antitrypsin (α1 -AT) serves as an archetypal example for the serine proteinase inhibitor (serpin) protein family and has been used as a scaffold for protein engineering for >35 years. Techniques used to engineer α1 -AT include targeted mutagenesis, protein fusions, phage display, glycoengineering, and consensus protein design. The goals of engineering have also been diverse, ranging from understanding serpin structure-function relationships, to the design of more potent or more specific proteinase inhibitors with potential therapeutic relevance. Here we summarize the history of these protein engineering efforts, describing the techniques applied to engineer α1 -AT, specific mutants of interest, and providing an appended catalog of the >200 α1 -AT mutants published to date.
3. Core skeletal muscle ryanodine receptor calcium release complex
Angela F Dulhunty, Lan Wei-LaPierre, Marco G Casarotto, Nicole A Beard Clin Exp Pharmacol Physiol. 2017 Jan;44(1):3-12. doi: 10.1111/1440-1681.12676.
The core skeletal muscle ryanodine receptor (RyR1) calcium release complex extends through three compartments of the muscle fibre, linking the extracellular environment through the cytoplasmic junctional gap to the lumen of the internal sarcoplasmic reticulum (SR) calcium store. The protein complex is essential for skeletal excitation-contraction (EC)-coupling and skeletal muscle function. Its importance is highlighted by perinatal death if any one of the EC-coupling components are missing and by myopathies associated with mutation of any of the proteins. The proteins essential for EC-coupling include the DHPR α1S subunit in the transverse tubule membrane, the DHPR β1a subunit in the cytosol and the RyR1 ion channel in the SR membrane. The other core proteins are triadin and junctin and calsequestrin, associated mainly with SR. These SR proteins are not essential for survival but exert structural and functional influences that modify the gain of EC-coupling and maintain normal muscle function. This review summarises our current knowledge of the individual protein/protein interactions within the core complex and their overall contribution to EC-coupling. We highlight significant areas that provide a continuing challenge for the field. Additional important components of the Ca2+ release complex, such as FKBP12, calmodulin, S100A1 and Stac3 are identified and reviewed elsewhere.

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L

* 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

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Tip: Chemical formula is case sensitive. C22H30N4O c22h30n40
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