추천 제품
분석
≥95% (LC/MS-ELSD)
형태
solid
응용 분야
metabolomics
vitamins, nutraceuticals, and natural products
저장 온도
−20°C
InChI
1S/C21H22O10/c22-8-16-18(26)19(27)20(28)21(31-16)29-11-5-12(24)17-13(25)7-14(30-15(17)6-11)9-1-3-10(23)4-2-9/h1-6,14,16,18-24,26-28H,7-8H2/t14-,16+,18+,19-,20+,21+/m0/s1
InChI key
DLIKSSGEMUFQOK-SFTVRKLSSA-N
일반 설명
Natural product derived from plant source.
신호어
Warning
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Aquatic Acute 1 - Aquatic Chronic 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
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.
Plant molecular biology, 27(1), 205-210 (1995-01-01)
A number of different cDNA clones corresponding to the most abundant mRNAs present in immature seeds have been isolated from an almond (Prunus amygdalus cv. Texas) immature seed cDNA library. Those corresponding to proteins involved in storage processes have been
Planta medica, 57(3), 208-211 (1991-06-01)
Blood glucose and total lipid levels in rats with streptozotocin-induced diabetes were determined after intraperitoneal administration of a methanolic extract of Prunus davidiana Fr. stems and its main component, prunin (= naringenin 7-O-beta-D-glucoside). From the data obtained it was concluded
Analytical biochemistry, 134(2), 393-397 (1983-10-15)
A naringinase assay capable of distinguishing between the content of naringin, prunin, and naringenin present in the incubation mixture, is described. The amount of these compounds can be estimated by combining two spectrophotometric procedures. (a) Treatment with strong alkali to
Molecular immunology, 55(3-4), 253-263 (2013-03-19)
Tree nuts are a widely consumed food. Although enjoyed safely by most individuals, allergic reactions to tree nuts, including almond, are not uncommon. Almond prunin (Pru du 6), an 11S globulin (legumin), is an abundant nut seed protein and a
Bioscience, biotechnology, and biochemistry, 66(7), 1442-1449 (2002-09-13)
The kinetics of thermal inactivation of A. terreus alpha-rhamnosidase was studied using the substrate p-nitrophenyl alpha-L-rhamnoside between 50 degrees C and 70 degrees C. Up to 60 degrees C the inactivation of the purified enzyme was completely reversible, but samples
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