추천 제품
설명
13C-depleted
동위원소 순도
99.9 atom % 12C
광학 활성
[α]25/D +14.5°, c = 2 in 1 M HCl
재고 정보
available only in Japan
mp
314.5 °C (dec.) (lit.)
질량 이동
depleted
SMILES string
[12CH3][12C@H](N)[12C](O)=O
InChI
1S/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1/i1+0,2+0,3+0
InChI key
QNAYBMKLOCPYGJ-BWIFZRRMSA-N
관련 카테고리
생화학적/생리학적 작용
L-Alanine is a nonessential amino acid, which is highly concentrated in muscle. It is a key player in the Glucose-Alanine cycle, which enables the removal of pyruvate and glutamate from muscle to the liver. Once in the liver, glucose is regenerated from pyruvate and returned to the muscle while glutamate ultimately participates in the urea cycle to form urea. The Glucose-Alanine cycle aides to conserve ATP in muscle for muscle contraction, while the energy burden of gluconeogenesis is imposed upon the liver. Alanine inhibits pyruvate kinase to regulate gluconeogenesis and glycolysis in order to maintain glucose homeostasis during starvation. Alanine prevents hepatic autophagy. Alanine formation is a result of transamination of glutamate and pyruvate.
포장
This product may be available from bulk stock and can be packaged on demand. For information on pricing, availability and packaging, please contact Stable Isotopes Customer Service.
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
Alanine and glutamine synthesis and release from skeletal muscle. II. The precursor role of amino acids in alanine and glutamine synthesis.
The Journal of Biological Chemistry, 251(3), 836-843 (1976)
Muscle alanine synthesis and hepatic gluconeogenesis
Biochemical Society Transactions, 8(2), 205-213 (1980)
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Nucleic acids research, 42(6), 3943-3953 (2013-12-29)
Errors in protein synthesis due to mispairing of amino acids with tRNAs jeopardize cell viability. Several checkpoints to prevent formation of Ala- and Cys-tRNA(Pro) have been described, including the Ala-specific editing domain (INS) of most bacterial prolyl-tRNA synthetases (ProRSs) and
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