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Methyl-2-amino-3-hydroxypropanoate hydrochloride ≥98.0% (by total nitrogen and titration analysis)

Leverandør: TCI

Beskrivelse: Methyl-2-amino-3-hydroxypropanoate hydrochloride ≥98.0% (by total nitrogen and titration analysis)

Benserazide hydrochloride ≥97.0% (by HPLC, titration analysis)

Leverandør: TCI

Beskrivelse: Benserazide hydrochloride ≥97.0% (by HPLC, titration analysis)

DL-Serin

Varenummer: (EHERC16935700)

Leverandør: EHRENSTORFER

Beskrivelse: DL-Serin

UOM: 1 * 0,1 g

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DL-Serin (not of animal origin) 98,5+% (dry basis)

Leverandør: Thermo Fisher Scientific

Beskrivelse: DL-Serin (not of animal origin) 98,5+% (dry basis)

DL-Serin ≥98%, white powder

Leverandør: MP Biomedicals

Beskrivelse: NMDA agonist acting at the glycine site; precursor of glycine by serine hydroxymethyltransferase.

Nα-(p-Toluenesulphonyl)-DL-lysine chloromethyl ketone hydrochloride ≥95% (by elemental analysis), off-white solid, Calbiochem®

Leverandør: Merck Millipore (Calbiochem‎)

Beskrivelse: Inhibits trypsin-like serine proteinases.

Anti-SERPINA1 Mouse Monoclonal Antibody [clone: AAT/1379]

Varenummer: (PRSI33-599)

Leverandør: ProSci Inc.

Beskrivelse: Alpha-1 Antitrypsin or alpha1-antitrypsin (A1AT) is a protease inhibitor belonging to the serpin superfamily. It is generally known as serum trypsin inhibitor. Alpha 1-antitrypsin is also referred to as alpha-1 proteinase inhibitor (A1PI) because it inhibits a wide variety of proteases. It protects tissues from enzymes of inflammatory cells, especially neutrophil elastase, and has a reference range in blood of 1.5 - 3.5 gram/liter (in US the reference range is generally expressed as mg/dL or micromoles), but the concentration can rise manyfold upon acute inflammation. In its absence (such as in alpha 1-antitrypsin deficiency), neutrophil elastase is free to break down elastin, which contributes to the elasticity of the lungs, resulting in respiratory complications such as emphysema, or COPD (chronic obstructive pulmonary disease) in adults and cirrhosis in adults or children.<p>Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. Mutations in these areas can lead to non-functional proteins that can polymerise and accumulate in the liver (infantile hepatic cirrhosis). [Wiki].

UOM: 1 * 1 Each

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