Cat: PA2000-8245

Recombinant Human HIF3A Protein,His

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Analytical Data

  • Gene name

    HIF3A

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Basic-helix-loop-helix-PAS protein MOP7; bHLHe17; Class E basic helix-loop-helix protein 17; HIF 3A; HIF 3A4; HIF-3-alpha; HIF3 alpha; HIF3-alpha; HIF3-alpha-1; HIF3A; HIF3A_HUMAN; Hypoxia Inducible Factor 3 alpha; Hypoxia inducible factor 3 alpha subunit; Hypoxia inducible factor three alpha ; Hypoxia-inducible factor 3-alpha; Inhibitory PAS domain protein; IPAS; Member of PAS protein 7; MOP7; PAS domain-containing protein 7; PASD7

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9Y2N7

  • Expression Region

    1-669aa

  • AA Sequence

    MALGLQRARS TTELRKEKSR DAARSRRSQE TEVLYQLAHT LPFARGVSAH LDKASIMRLT ISYLRMHRLC AAGEWNQVGA GGEPLDACYL KALEGFVMVL TAEGDMAYLS ENVSKHLGLS QLELIGHSIF DFIHPCDQEE LQDALTPQQT LSRRKVEAPT ERCFSLRMKS TLTSRGRTLN LKAATWKVLN CSGHMRAYKP PAQTSPAGSP DSEPPLQCLV LICEAIPHPG SLEPPLGRGA FLSRHSLDMK FTYCDDRIAE VAGYSPDDLI GCSAYEYIHA LDSDAVSKSI HTLLSKGQAV TGQYRFLARS GGYLWTQTQA TVVSGGRGPQ SESIVCVHFL ISQVEETGVV LSLEQTEQHS RRPIQRGAPS QKDTPNPGDS LDTPGPRILA FLHPPSLSEA ALAADPRRFC SPDLRRLLGP ILDGASVAAT PSTPLATRHP QSPLSADLPD ELPVGTENVH RLFTSGKDTE AVETDLDIAQ DADALDLEML APYISMDDDF QLNASEQLPR AYHRPLGAVP RPRARSFHGL SPPALEPSLL PRWGSDPRLS CSSPSRGDPS ASSPMAGARK RTLAQSSEDE DEGVELLGVR PPKRSPSPEH ENFLLFPLSL SFLLTGGPAP GSLQDPSTPL LNLNEPLGLG PSLLSPYSDE DTTQPGGPFQ PRAGSAQAD

  • Molecular Weight

    72.4 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.

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Protein Description

HIF3A, or Hypoxia-Inducible Factor 3 Alpha, is a key member of the hypoxia-inducible factor (HIF) family of transcription factors, which play essential roles in cellular responses to low oxygen levels (hypoxia). Unlike its better-known counterparts, HIF-1α and HIF-2α, HIF3A is less understood but is believed to have both regulatory and protective roles in various physiological and pathological processes. Research into HIF3A has gained traction due to its potential implications in various diseases, including cancer, where altered oxygen sensing and signaling can contribute to tumor growth and metastasis. Additionally, HIF3A has been implicated in metabolic disorders and cardiovascular diseases. The ability to leverage recombinant HIF3A proteins for functional studies is pivotal for elucidating its biological activities, regulatory mechanisms, and interaction with other proteins within the hypoxia response pathway. This may aid in the development of therapeutic strategies targeting HIF signaling, providing insights into how manipulation of HIF3A could contribute to innovative treatments for hypoxia-related diseases. Understanding the structure and function of HIF3A at the molecular level through recombinant protein studies may reveal its unique roles and potential as a drug target, thereby highlighting the importance of this research in advancing our knowledge of cellular adaptation to environmental stressors.

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