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Merck
모든 사진(4)

문서

A7094

Sigma-Aldrich

L-Asparagine monohydrate

≥98.0%, suitable for cell culture, BioReagent, non-animal source

동의어(들):

Asparagine monohydrate, (S)-(+)-2-Aminosuccinamic acid, (S)-2-Aminosuccinic acid 4-amide, L-Aspartic acid 4-amide

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About This Item

Linear Formula:
NH2COCH2CH(NH2)COOH · H2O
CAS Number:
Molecular Weight:
150.13
Beilstein:
1723527
EC Number:
MDL number:
UNSPSC 코드:
12352209
PubChem Substance ID:
NACRES:
NA.26

product name

L-Asparagine monohydrate, from non-animal source, BioReagent, suitable for cell culture, ≥98.0%

생물학적 소스

non-animal source

제품 라인

BioReagent

분석

≥98.0%

형태

powder

광학 활성

[α]20/D 33.0 to 36.3 °, c = 10 in 6 M HCl

기술

cell culture | mammalian: suitable

불순물

endotoxin, tested

색상

white

mp

233-235 °C (lit.)

solubility

H2O: 20 mg/mL

양이온 미량물

Fe: ≤10 ppm
heavy metals (as Pb): ≤10 ppm
<0.1% (Ammonia (NH3))

작용기

amide
amine
carboxylic acid

저장 온도

room temp

SMILES string

[H]O[H].N[C@@H](CC(N)=O)C(O)=O

InChI

1S/C4H8N2O3.H2O/c5-2(4(8)9)1-3(6)7;/h2H,1,5H2,(H2,6,7)(H,8,9);1H2/t2-;/m0./s1

InChI key

RBMGJIZCEWRQES-DKWTVANSSA-N

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일반 설명

L-Asparagine is a naturally occurring amino acid found in various proteins. It is used in laboratory research for various applications, including cell culture, protein biochemistry, and nitrogen metabolism studies. Its solubility in water and role as a source of asparagine make it a versatile tool for investigating biological processes and chemical synthesis. Further, L-Asparagine residues in proteins can be crucial for protein stability, folding, and interactions.

애플리케이션

L-Asparagine is used in cell culture media and is a component of MEM non-essential amino acids solution. L-Asparagine has been shown to enhance ornithine decarboxylase activity in cultured human colon adenocarcinoma Caco-2 cells and in cultured IEC-6 intestinal epithelial cells. Spore germination in Bacillus subtilis has been increased in the presence of L-asparagine. L-Asparagine, a proteinogenic amino acid, from non-animal source is used in biomanufacturing cell culture systems for the production of therapeutic recombinant proteins and monoclonal antibodies. It has also been used as a component of LHC basal media for the culture of human airway epithelial cells.

생화학적/생리학적 작용

The amino acid L-asparagine is a structural analog of L-aspartic acid, where the side chain of the carboxylic acid moiety is amidated to give a terminal amine group. This renders L-asparagine neutral at physiological pH. The amide group of asparagine is derived from glutamine, in the reaction of aspartate and glutamine in the presence of ATP to yield asparagine and glutamate. In vivo, asparagine is hydrolyzed to aspartate and NH4+ by asparaginase. Asparagine is also an important amino acid in glycopeptide bonds, via N-glycosyl linkages to the sugar rings.

특징 및 장점

  • Suitable for Cell Culture and Biochemical research
  • High-quality compound suitable for multiple research applications

기타 정보

For additional information on our range of Biochemicals, please complete this form.

관련 제품

제품 번호
설명
가격

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

Handbook of Chem-ical Neu-roanatomy (2014)
Methods in Molecular Medicine, 107 null
T Berg et al.
Molecular genetics and metabolism, 73(1), 18-29 (2001-05-15)
Lysosomal alpha-mannosidase (EC 3.2.1.24) is required in the degradation of the asparagine-linked carbohydrates of glycoproteins. Deficiency of this enzyme leads to the lysosomal storage disorder alpha-mannosidosis. As an initial step toward enzyme replacement therapy for alpha-mannosidosis, the human lysosomal alpha-mannosidase
G B Nyberg et al.
Biotechnology and bioengineering, 62(3), 336-347 (1999-04-01)
Asparagine linked (N-linked) glycosylation is an important modification of recombinant proteins, because the attached oligosaccharide chains can significantly alter protein properties. Potential glycosylation sites are not always occupied with oligosaccharide, and site occupancy can change with the culture environment. To
Stryer L
Biochemistry (2002)

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