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L-Asparagine

$43

  • Brand : BIOFRON

  • Catalogue Number : BF-L2006

  • Specification : 98%

  • CAS number : 70-47-3

  • Formula : C4H8N2O3

  • Molecular Weight : 132.12

  • Volume : 20mg

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Catalogue Number

BF-L2006

Analysis Method

HPLC,NMR,MS

Specification

98%

Storage

2-8°C

Molecular Weight

132.12

Appearance

White crystalline powder

Botanical Source

Glycine max

Structure Type

Others

Category

SMILES

C(C(C(=O)O)N)C(=O)N

Synonyms

IUPAC Name

Density

1.4±0.1 g/cm3

Solubility

H2O : 6.67 mg/mL (50.48 mM; Need ultrasonic)

Flash Point

218.7±27.3 °C

Boiling Point

438.0±40.0 °C at 760 mmHg

Melting Point

235 °C (dec.)(lit.)

InChl

InChI=1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1

InChl Key

DCXYFEDJOCDNAF-REOHCLBHSA-N

WGK Germany

RID/ADR

HS Code Reference

2924190000

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:70-47-3) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

PMID

32034141

Abstract

The conserved hemagglutinin (HA) stem has been a focus of universal influenza vaccine efforts. Influenza A group 1 HA stem-nanoparticles have been demonstrated to confer heterosubtypic protection in animals; however, the protection does not extend to group 2 viruses, due in part to differences in glycosylation between group 1 and 2 stems. Here, we show that introducing the group 2 glycan at Asn38HA1 to a group 1 stem-nanoparticle (gN38 variant) based on A/New Caledonia/20/99 (H1N1) broadens antibody responses to cross-react with group 2 HAs. Immunoglobulins elicited by the gN38 variant provide complete protection against group 2 H7N9 virus infection, while the variant loses protection against a group 1 H5N1 virus. The N38HA1 glycan thus is pivotal in directing antibody responses by controlling access to group-determining stem epitopes. Precise targeting of stem-directed antibody responses to the site of vulnerability by glycan repositioning may be a step towards achieving cross-group influenza protection.

Title

Glycan Repositioning of Influenza Hemagglutinin Stem Facilitates the Elicitation of Protective Cross-Group Antibody Responses

Author

Seyhan Boyoglu-Barnum 1, Geoffrey B Hutchinson 1, Jeffrey C Boyington 1, Syed M Moin 1, Rebecca A Gillespie 1, Yaroslav Tsybovsky 2, Tyler Stephens 2, John R Vaile 1, Julia Lederhofer 1, Kizzmekia S Corbett 1, Brian E Fisher 1, Hadi M Yassine 3, Sarah F Andrews 1, Michelle C Crank 1, Adrian B McDermott 1, John R Mascola 1, Barney S Graham 4, Masaru Kanekiyo 5

Publish date

2020 Feb 7

PMID

31911207

Title

Selective Pressure on an Interfacial Enzyme: Functional Roles of a Highly Conserved Asparagine Residue in a Cellulase

Author

Trine Holst Sørensen 1, Silke Flindt Badino 2, Michael Skovbo Windahl 1, Nanna Røjel 2, Brett McBrayer 3, Kim Borch 1, Peter Westh 4

Publish date

2020 Mar

PMID

31871197

Abstract

Mechanosensitive ion channels are crucial for normal cell function and facilitate physiological function, such as blood pressure regulation. So far little is known about the molecular mechanisms of how channels sense mechanical force. Canonical vertebrate epithelial Na+ channel (ENaC) formed by α-, β-, and γ-subunits is a shear force (SF) sensor and a member of the ENaC/degenerin protein family. ENaC activity in epithelial cells contributes to electrolyte/fluid-homeostasis and blood pressure regulation. Furthermore, ENaC in endothelial cells mediates vascular responsiveness to regulate blood pressure. Here, we provide evidence that ENaC’s ability to mediate SF responsiveness relies on the “force-from-filament” principle involving extracellular tethers and the extracellular matrix (ECM). Two glycosylated asparagines, respectively their N-glycans localized in the palm and knuckle domains of αENaC, were identified as potential tethers. Decreased SF-induced ENaC currents were observed following removal of the ECM/glycocalyx, replacement of these glycosylated asparagines, or removal of N-glycans. Endothelial-specific overexpression of αENaC in mice induced hypertension. In contrast, expression of αENaC lacking these glycosylated asparagines blunted this effect. In summary, glycosylated asparagines in the palm and knuckle domains of αENaC are important for SF sensing. In accordance with the force-from-filament principle, they may provide a connection to the ECM that facilitates vascular responsiveness contributing to blood pressure regulation.

KEYWORDS

N-glycosylation; epithelial Na+ channel (ENaC); extracellular tether; mechanotransduction; shear force.

Title

Shear Force Sensing of Epithelial Na + Channel (ENaC) Relies on N-glycosylated Asparagines in the Palm and Knuckle Domains of αENaC

Author

Fenja Knoepp 1, Zoe Ashley 2 3, Daniel Barth 2 3, Jan-Peter Baldin 2 3, Michael Jennings 2, Marina Kazantseva 2, Eng Leng Saw 2 3, Rajesh Katare 2 3, Diego Alvarez de la Rosa 4, Norbert Weissmann 1, Martin Fronius 5 3

Publish date

2020 Jan 7


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