{"product_id":"recombinant-human-egl-nine-homolog-2egln2-partial","title":"Recombinant Human Egl nine homolog 2(EGLN2),partial","description":"\u003cp\u003e\u003cb\u003eSize\u003c\/b\u003e: 200ug. Other sizes are also available. Please Inquire.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eIn Stock\u003c\/b\u003e: No\u003c\/p\u003e\u003cp\u003e\u003cb\u003eLead time\u003c\/b\u003e: 10-20 working days\u003c\/p\u003e\u003cp\u003e\u003cb\u003eResearch Topic\u003c\/b\u003e: Cancer\u003c\/p\u003e\u003cp\u003e\u003cb\u003eUniprot ID\u003c\/b\u003e: Q96KS0\u003c\/p\u003e\u003cp\u003e\u003cb\u003eGene Names\u003c\/b\u003e: EGLN2\u003c\/p\u003e\u003cp\u003e\u003cb\u003eOrganism\u003c\/b\u003e: Homo sapiens (Human)\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAA Sequence\u003c\/b\u003e: MVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT\u003c\/p\u003e\u003cp\u003e\u003cb\u003eExpression Region\u003c\/b\u003e: 283-407aa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eSequence Info\u003c\/b\u003e: Partial\u003c\/p\u003e\u003cp\u003e\u003cb\u003eSource\u003c\/b\u003e: E.coli\u003c\/p\u003e\u003cp\u003e\u003cb\u003eTag Info\u003c\/b\u003e: N-terminal 6xHis-tagged\u003c\/p\u003e\u003cp\u003e\u003cb\u003eMW\u003c\/b\u003e: 18.1 kDa\u003c\/p\u003e\u003cp\u003e\u003cb\u003eAlternative Name(s)\u003c\/b\u003e: Estrogen-induced tag 6HPH-3Hypoxia-inducible factor prolyl hydroxylase 1 ;HIF-PH1 ;HIF-prolyl hydroxylase 1 ;HPH-1;Prolyl hydroxylase domain-containing protein 1 ;PHD1\u003c\/p\u003e\u003cp\u003e\u003cb\u003eRelevance\u003c\/b\u003e: 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 HIF2A. 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. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferencially recognized via a LXXLAP motif.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eReference\u003c\/b\u003e: The DNA sequence and biology of human chromosome 19.Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.  , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.Nature 428:529-535(2004)\u003c\/p\u003e\u003cp\u003e\u003cb\u003ePurity\u003c\/b\u003e: Greater than 90% as determined by SDS-PAGE.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eStorage Buffer\u003c\/b\u003e: Tris-based buffer，50% glycerol \u003c\/p\u003e\u003cp\u003e\u003cb\u003eStorage\u003c\/b\u003e: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. \nGenerally, the shelf life of liquid form is 6 months at -20℃\/-80℃. The shelf life of lyophilized form is 12 months at -20℃\/-80℃.\u003c\/p\u003e\u003cp\u003e\u003cb\u003eNotes\u003c\/b\u003e: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.\u003c\/p\u003e","brand":"Gene Bio Systems","offers":[{"title":"Default Title","offer_id":39766722248804,"sku":"CSB-EP007482HU","price":680.95,"currency_code":"EUR","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0558\/8588\/9636\/products\/no_image_default_image-jpeg_dcb2bb38-d3d9-46e0-a5ba-ccc49c276927.jpg?v=1659191218","url":"https:\/\/www.genebiosystems.com\/en-de\/products\/recombinant-human-egl-nine-homolog-2egln2-partial","provider":"GeneBio ","version":"1.0","type":"link"}