Cat: PA2000-9841

Recombinant Human OGFOD1 Protein,His

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Analytical Data

  • Gene name

    OGFOD1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    2 oxoglutarate and iron dependent oxygenase domain containing 1; 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1; FLJ10826; KIAA1612; OGFD1_HUMAN; OGFOD1; Termination and polyadenylation 1 homolog; TPA1; TPA1 termination and polyadenylation 1 homolog

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8N543

  • Expression Region

    1-542 aa

  • AA Sequence

    MNGKRPAEPG PARVGKKGKK EVMAEFSDAV TEETLKKQVA EAWSRRTPFS HEVIVMDMDP FLHCVIPNFI QSQDFLEGLQ KELMNLDFHE KYNDLYKFQQ SDDLKKRREP HISTLRKILF EDFRSWLSDI SKIDLESTID MSCAKYEFTD ALLCHDDELE GRRIAFILYL VPPWDRSMGG TLDLYSIDEH FQPKQIVKSL IPSWNKLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP SLTRPPNYFE PPIPRSPHIP QDHEILYDWI NPTYLDMDYQ VQIQEEFEES SEILLKEFLK PEKFTKVCEA LEHGHVEWSS RGPPNKRFYE KAEESKLPEI LKECMKLFRS EALFLLLSNF TGLKLHFLAP SEEDEMNDKK EAETTDITEE GTSHSPPEPE NNQMAISNNS QQSNEQTDPE PEENETKKES SVPMCQGELR HWKTGHYTLI HDHSKAEFAL DLILYCGCEG WEPEYGGFTS YIAKGEDEEL LTVNPESNSL ALVYRDRETL KFVKHINHRS LEQKKTFPNR TGFWDFSFIY YE

  • Molecular Weight

    63.2 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

OGFOD1 (Oxygen-Dependent Fumarate Hydratase Domain 1) is a protein that has garnered attention due to its potential role in various biological processes, particularly in cellular response to hypoxia and regulation of protein stability. Studies have indicated that OGFOD1 acts as a novel dioxygenase, which modifies hypoxia-induced factors, thus influencing cellular pathways related to adaptation to low oxygen levels. The protein has also been implicated in several pathophysiological conditions, including cancer, where it may play a role in tumor progression and metastasis. The understanding of OGFOD1's function is further complicated by its involvement in the post-translational modification of proteins, particularly by affecting the hydroxylation of proline residues, which is crucial for the stability and function of numerous proteins. This has led to increased interest in OGFOD1 as a potential therapeutic target for diseases characterized by altered oxygen sensing or signaling pathways. As researchers explore the biochemical properties and interactions of OGFOD1, the characterization of its recombinant form has become essential for elucidating its functional mechanisms. This research not only provides insights into the fundamental roles of OGFOD1 in cellular physiology but also opens avenues for developing novel therapeutic strategies aimed at modulating its activity in disease contexts. Overall, the study of OGFOD1 and its recombinant protein is critical for advancing our understanding of cellular adaptability and the molecular basis of diseases associated with oxygen homeostasis.

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