Cat: PA1000-3858

Recombinant Human VEGFD Protein,His

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Analytical Data

  • Gene name

    VEGFD

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    VEGFD;FIGF;Vascular endothelial growth factor D

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O43915

  • Expression Region

    93-201aa

  • AA Sequence

    FYDIETLKVI DEEWQRTQCS PRETCVEVAS ELGKSTNTFF KPPCVNVFRC GGCCNEESLI CMNTSTSYIS KQLFEISVPL TSVPELVPVK VANHTGCKCL PTAPRHPYS

  • Molecular Weight

    14 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

VEGFD (Vascular Endothelial Growth Factor D) is a member of the VEGF family, which plays a crucial role in the formation of blood vessels and lymphatic systems. Its primary function is to promote endothelial cell proliferation and survival, primarily in response to hypoxic conditions. Research into VEGFD has gained significance due to its implications in various physiological and pathological processes, including angiogenesis, lymphangiogenesis, and cancer progression. Elevated levels of VEGFD have been associated with several malignancies, where it contributes to tumor growth and metastasis by enhancing lymphatic vessel formation and facilitating tumor cell dissemination. Furthermore, its role in non-cancerous conditions like inflammation and tissue repair underscores its potential as a therapeutic target. Given the complexity of VEGF signaling pathways, ongoing studies are focused on elucidating VEGFD’s mechanisms of action, interactions with other molecules, and its regulatory networks within the tumor microenvironment. Recombinant VEGFD protein studies are particularly important as they provide insights into its biological functions and enable the development of diagnostic and therapeutic applications, potentially leading to novel treatments for diseases related to vascular dysregulation. The exploration of VEGFD's properties has implications for the understanding of not only cancer biology but also other conditions characterized by abnormal vascular growth, making it a vital area of inquiry in contemporary biomedical research.

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