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Merck

12685

Sigma-Aldrich

Nω-磷酸-L-精氨酸 锂盐 水合物

≥95.0% (TLC)

别名:

H-Arg(PO3H2)-OH lithium salt, N5-(Phosphonoamidino)-L-ornithine lithium salt, N5-[Imino(phosphonoamino)methyl]-L-ornithine lithium salt, L-2-Amino-5-(N′-phosphonoguanidino)valeric acid lithium salt, Lithium L-arginine phosphate

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About This Item

经验公式(希尔记法):
C6H15N4O5P · xLi+ · yH2O
CAS号:
分子量:
254.18 (free acid basis)
EC號碼:
分類程式碼代碼:
12352209
NACRES:
NA.26

化驗

≥95.0% (TLC)

形狀

powder or crystals

顏色

white to off-white

儲存溫度

−20°C

InChI

1S/C6H15N4O5P/c7-4(5(11)12)2-1-3-9-6(8)10-16(13,14)15/h4H,1-3,7H2,(H,11,12)(H5,8,9,10,13,14,15)/t4-/m0/s1

InChI 密鑰

CCTIOCVIZPCTGO-BYPYZUCNSA-N

生化/生理作用

Important metabolite in arginine and proline metabolism, high-energy metabolite, constituent of crustaceans and crayfish muscle.

分析報告

may contain 8% more water then theoretically in monohydrate expected

象形圖

Exclamation mark

訊號詞

Warning

危險聲明

危險分類

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

標靶器官

Respiratory system

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Gaspar E Canepa et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 160(1), 40-43 (2011-06-01)
Phytomonas are trypanosomatid plant parasites closely related to parasites that cause several human diseases. Little is known about the biology of these organisms including aspects of their metabolism. Arginine kinase (E.C. 2.7.3.3) is a phosphotransferase which catalyzes the interconversion between
Omar Davulcu et al.
Biochemistry, 50(19), 4011-4018 (2011-03-24)
Arginine kinase catalyzes the reversible transfer of a phosphoryl group between ATP and arginine. It is the arthropod homologue of creatine kinase, buffering cellular ATP levels. Crystal structures of arginine kinase, in substrate-free and substrate-bound forms, have revealed large conformational
Jonathan Bragg et al.
Journal of bacteriology, 194(10), 2668-2676 (2012-03-06)
Arginine kinases catalyze the reversible transfer of a high-energy phosphoryl group from ATP to l-arginine to form phosphoarginine, which is used as an energy buffer in insects, crustaceans, and some unicellular organisms. It plays an analogous role to that of
Margaret Werr et al.
Insect biochemistry and molecular biology, 39(9), 634-645 (2009-07-15)
Arginine kinase (ATP:l-arginine omega-N-phosphotransferase, EC2.7.3.3.; AK) is an enzyme crucial for the energy metabolism of insects and other invertebrates, that has known allergenic potential in humans and that has been proposed as a pesticidal drug target. Here we report the
Karina D García-Orozco et al.
International archives of allergy and immunology, 144(1), 23-28 (2007-05-15)
Consumption of seafood can produce allergic symptoms in susceptible individuals and crustacean allergies are the most frequently reported causes of allergic reactions. An allergen from the muscle of the white shrimp Litopenaeus vannamei was purified by ion exchange chromatography and

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