Cat: PA1000-8957

Recombinant Human ANG Protein,His

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Analytical Data

  • Gene name

    ANG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ANG;ANG3;ANG4;Angiopoietin-4

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P03950

  • Expression Region

    26-147aa

  • AA Sequence

    DNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP

  • Molecular Weight

    18.0kDa

  • 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

ANG (angiogenin) is a member of the ribonuclease A superfamily and plays a crucial role in various physiological processes, including angiogenesis, neuroprotection, and inflammation. Research into ANG and its restructured protein variants has gained momentum due to its potential therapeutic applications in cancer and neurodegenerative diseases. ANG is known for its ability to promote blood vessel formation, making it a central focus in studies aimed at understanding tumor progression and metastasis. Moreover, its neuroprotective properties have led to interest in its role in conditions such as amyotrophic lateral sclerosis (ALS) and Alzheimer's disease. Investigating the structure-function relationship of ANG through protein engineering and reconstitution techniques allows researchers to create modified forms with enhanced or altered biological activities. This manipulation of ANG can lead to the development of novel therapeutic agents that target specific pathways involved in disease progression. Furthermore, the study of ANG's interaction with RNA and its involvement in stress granule dynamics provides insights into the molecular mechanisms underlying its diverse functions. Overall, the research surrounding ANG restructured protein is vital for uncovering its therapeutic potential and understanding its multifaceted roles in health and disease.

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