Cat: IPD-X20569

Recombinant Human SIRP alpha/CD172a Protein(HEK293), Avi & His

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Analytical Data

  • Gene name

    SIRP alpha/CD172a

  • 简介

    The SIRP α V4/CD172a protein is an immunoglobulin-like cell surface receptor for CD47 that acts as a docking protein to facilitate the translocation of PTPN6, PTPN11, and other partners to the plasma membrane. It supports the adhesion of cerebellar neurons, promotes neurite growth, and promotes glial cell attachment. SIRP alpha/CD172a Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived SIRP alpha/CD172a protein, expressed by HEK293 , with C-Avi, C-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HP Substrate 1; SHPS-1; Bit; Sirp-Alpha-1; Sirp-Alpha-2; Sirp-Alpha-3; p84; CD172a; BIT; MFR; MYD1; PTPNS1; SHPS1; SIRP

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-Avi;C-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P78324-1

  • Expression Region

    E31-R370

  • AA Sequence

    EEELQVIQPDKSVLVAAGETATLRCTATSLIPVGPIQWFRGAGPGRELIYNQKEGHFPRVTTVSDLTKRNNMDFSIRIGNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAARATPQHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPVGESVSYSIHSTAKVVLTREDVHSQVICEVAHVTLQGDPLRGTANLSETIRVPPTLEVTQQPVRAENQVNVTCQVRKFYPQRLQLTWLENGNVSRTETASTVTENKDGTYNWMSWLLVNVSAHRDDVKLTCQVEHDGQPAVSKSHDLKVSAHPKEQGSNTAAENTGSNER

  • Protein Length

    Extracellular Domain

  • Molecular Weight

    50-80 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

SIRP alpha (Signal Regulatory Protein alpha), also known as CD172a, plays a critical role in regulating immune responses by interacting with the CD47 molecule, which is often referred to as the "don't eat me" signal. This interaction inhibits phagocytosis by macrophages and is crucial for maintaining self-tolerance and preventing autoimmunity. The study of SIRP alpha/CD172a recombinant proteins has gained prominence due to its potential therapeutic implications in cancer immunotherapy and autoimmune diseases. In tumors, cancer cells often overexpress CD47, allowing them to evade immune detection and destruction. By engineering SIRP alpha as a recombinant protein, researchers can block the CD47-SIRP alpha interaction, enhancing phagocytosis of cancer cells by macrophages and promoting anti-tumor immunity. Additionally, SIRP alpha/CD172a protein research provides insights into the mechanisms of immune regulation and has implications for designing novel immunotherapeutic strategies. The development of SIRP alpha/CD172a recombinant protein not only advances our understanding of immune checkpoint pathways but also opens new avenues for clinical applications in treating various malignancies and enhancing the effectiveness of existing immunotherapies. Moreover, the study of this protein contributes to a broader understanding of the immune system's regulation, potentially leading to breakthroughs in managing immune-related disorders.

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