AMD1 Protein (His tag)

Produktnummer ABIN1098638

Produktdetails

Target: AMD1 (Adenosylmethionine Decarboxylase 1 (AMD1))

Protein-Typ: Recombinant

Spezies: Human

Quelle: Escherichia coli (E. coli)

Aufreinigungstag / Konjugat: Dieses AMD1 Protein ist gelabelt mit His tag.

Applikation: SDS-PAGE (SDS)

Aufreinigung: purified by using conventional chromatography.

Reinheit: > 80 % by SDS - PAGE

Anwendungsinformationen

Kommentare:

Synonyms: S-adenosylmethionine decarboxylase proenzyme, ADOMETDC, AMD, DKFZp313L1234, FLJ26964, SAMDC

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: 0.5 mg/ml (determined by Bradford assay)

Buffer: 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 0.1 M NaCl, 1 MM DTT

Lagerung: 4 °C

Informationen zur Lagerung: Avoid repeated freezing and thawing cycles.

Antigendetails

Target: AMD1 (Adenosylmethionine Decarboxylase 1 (AMD1))

Andere Bezeichnung: AMD1 (AMD1 Produkte)

Synonyme: ADOMETDC Protein, AMD Protein, SAMDC Protein, Amd1a Protein, Amd1b Protein, AMD1 Protein, AdoMetDC Protein, amd Protein, samdc Protein, fb26e03 Protein, si:ch211-257g8.2 Protein, wu:fb26e03 Protein, zgc:55614 Protein, 1 Protein, Amd-1 Protein, SAMDC 1 Protein, adoMetDC1 Protein, CG5029 Protein, Dmel\\CG5029 Protein, l(2)31Dc Protein, l(2)31Dd Protein, l(2)31De Protein, F16B3.10 Protein, F16B3_10 Protein, S-ADENOSYLMETHIONINE DECARBOXYLASE Protein, S-adenosylmethionine decarboxylase Protein, adenosylmethionine decarboxylase 1 Protein, S-adenosylmethionine decarboxylase 1 Protein, S-adenosyl methionine decarboxylase 2 Protein, adenosylmethionine decarboxylase 1 L homeolog Protein, S-adenosylmethionine decarboxylase Protein, AMD1 Protein, Amd1 Protein, amd1 Protein, sam2 Protein, amd1.L Protein, SamDC Protein, SAMDC Protein

Hintergrund: AMD1, also known as adenosylmethionine decarboxylase proenzyme, is synthesized initially as an inactive proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. Recombinant human AMD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.

Molekulargewicht: 33.4 kDa (292aa) confirmed by MALDI-TOF

NCBI Accession: NP_001625

Pathways: Ribonucleoside Biosynthetic Process