Egl nine homolog 1 (EGLN1), partial, human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 177-426aa. Protein Length: Partial. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: GGLRPNGQTK PLPALKLALE YIVPCMNKHG ICVVDDFLGK ETGQQIGDEV RALHDTGKFT DGQLVSQKSD SSKDIRGDKI TWIEGKEPGC ETIGLLMSSM DDLIRHCNGK LGSYKINGRT KAMVACYPGN GTGYVRHVDN PNGDGRCVTC IYYLNKDWDA KVSGGILRIF PEGKAQFADI EPKFDRLLFF WSDRRNPHEV QPAYATRYAI TVWYFDADER ARAKVKYLTG EKGVRVELNK PSDSVGKDVF. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. Reference: "Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor." Hirsila M., Koivunen P., Gunzler V., Kivirikko K.I., Myllyharju J. J. Biol. Chem. 278:30772-30780(2003). Function: nan