Cat: IPD-X33102

Recombinant Rat VEGFR-1 Protein (HEK293),His

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Analytical Data

  • Gene name

    VEGFR-1

  • 简介

    VEGFR-1 protein is a tyrosine protein kinase receptor for VEGFA, VEGFB, and PGF and is critical for embryonic vasculature development, angiogenesis, cell survival, migration, macrophage function, chemotaxis, and cancer invasion. It actively regulates postnatal retinal vitreous vascular degeneration and may act as a negative regulator of embryonic angiogenesis. VEGFR-1 Protein, Rat (HEK293, His) is the recombinant rat-derived VEGFR-1 protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured by its binding ability in a functional ELISA. Immobilized Human VEGF165 at 0.1 μg/mL(100 μL/well) can bind biotinylated Rat VEGFR-1. The ED50 for this effect is 76.55 ng/mL. Measured by its binding ability in a functional ELISA. Immobilized Human VEGF165 at 0.1 μg/mL (100 μL/well) can bind biotinylated Rat VEGFR-1. The ED50 for this effect is 76.55 ng/mL.

  • Alternative Names

    Vascular endothelial growth factor receptor 1; FLT; FLT1; FRT; VEGFR-1

  • Species

    Rat

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P53767

  • Expression Region

    Y23-E758

  • AA Sequence

    YCSGSKLKGPELSLKGTQHVMQAGQTLFLKCRGEAAHSWSLPTTVSQEDKKLSVTRSACGRNNRQFCSTLTLNMAQANHTGLYSCRYLPKSTSKEKKMESAIYIFVSDAGSPFIEMHSDIPKLVHMTEGRELIIPCRVTSPNITVTLKKFPFDALTPDGQRIAWDSRRGFIIANATYKEIGLLTCEATVNGHLYQTSYLTHRQTNTILDVQISPPSPVRFLRGQTLVLNCTVTTDLNTRVQMSWNYPGKATKRASIRQRIDQSNPHSNVFHSVLKINNVESRDKGLYTCRVKSGSSFRTFNTSVHVYEKGFISVKHRKQQVQETIAGKRSHRLSMKVKAFPSPEVVWLKDGVPATEKSARYSVHGYSLIIKDVTAEDAGDYTILLGIKQSKLFRNLTATLIVNVKPQIYEKSVSSLPSPPLYPLGSRQVLTCTVYGIPQPTIKWLWHPCHYNHSKERNDFCFGSEESFILDSSSNIGNRIEGITQRMMVIEGTNKTVSTLVVADSRTPGSYSCKAFNKIGTVERDIRFYVTDVPNGFHVSLEKIPTEGEDLKLSCVVSKFLYRDITWILLRTVNNRTMHHSISKQKMATTQDYSITLNLVIKNVSLEDSGTYACRARNIYTGEEILRKTEVLVRDLEAPLLLQNLSDHEVSISGSTTLDCQARGVPAPQITWFKNNHKIQQEPGIILGPGNSTLFIERVTEEDEGVYRCRATNQKGVVESSAYLTVQGTSDKSNLE

  • Protein Length

    Extracellular Domain

  • Molecular Weight

    110-130 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

Vascular Endothelial Growth Factor Receptor 1 (VEGFR-1) is a critical receptor involved in angiogenesis, the formation of new blood vessels from pre-existing ones, which plays a significant role in various physiological and pathological processes, including cancer progression, tissue repair, and embryonic development. The overexpression of VEGFR-1 has been associated with tumor growth and metastasis, making it a potential target for cancer therapy. Research on recombinant VEGFR-1 proteins has surged as scientists aim to better understand its structure, function, and mechanisms of action. These studies often involve the production of recombinant VEGFR-1 proteins in various expression systems, allowing for in-depth analysis of their biochemical properties, ligand-binding abilities, and downstream signaling pathways. By elucidating the interactions between VEGFR-1 and its ligands, researchers hope to identify novel therapeutic strategies, including monoclonal antibodies or small-molecule inhibitors that can disrupt VEGFR-1 signaling, potentially leading to improved clinical outcomes in cancer treatment and other diseases linked to aberrant angiogenesis. Moreover, recombinant VEGFR-1 proteins serve as valuable tools for screening and development of anti-angiogenic drugs, providing insights into their efficacy and safety profiles. Overall, the study of recombinant VEGFR-1 not only enhances our understanding of vascular biology but also opens avenues for innovative therapeutic approaches targeting angiogenesis-related disorders.

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