Analytical Data
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Gene name
SIRPA
- Application
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Alternative Names
CD47;MER6;Leukocyte surface antigen CD47
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P78324
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Expression Region
31-370aa
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AA Sequence
EEELQVIQPDKSVLVAAGETATLRCTATSLIPVGPIQWFRGAGPGRELIY NQKEGHFPRVTTVSDLTKRNNMDFSIRIGNITPADAGTYYCVKFRKGSPD DVEFKSGAGTELSVRAKPSAPVVSGPAARATPQHTVSFTCESHGFSPRDI TLKWFKNGNELSDFQTNVDPVGESVSYSIHSTAKVVLTREDVHSQVICEV AHVTLQGDPLRGTANLSETIRVPPTLEVTQQPVRAENQVNVTCQVRKFYP QRLQLTWLENGNVSRTETASTVTENKDGTYNWMSWLLVNVSAHRDDVKLT CQVEHDGQPAVSKSHDLKVSAHPKEQGSNTAAENTGSNER
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Molecular Weight
64 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
SIRPA (Innate Immune Receptor Protein A) is a crucial receptor predominantly expressed on myeloid cells, playing a significant role in the regulation of immune responses. This receptor mediates various cellular processes, including phagocytosis and the regulation of immune signaling pathways, particularly through its interaction with the CD47 "don't eat me" signal, which inhibits macrophage-mediated phagocytosis of self-cells. Recent studies have highlighted the potential of SIRPA as a therapeutic target in cancer immunotherapy, as blocking the CD47-SIRPA interaction can enhance the clearance of tumor cells by the immune system. Furthermore, the understanding of SIRPA's structural biology and its downstream signaling mechanisms is essential for the development of engineered SIRPA proteins or antibodies that can boost anti-tumor immunity. By investigating the recombinant SIRPA protein, researchers aim to elucidate its functional properties and further explore its applications in both basic immunology and clinical settings. The insightful manipulation of SIRPA could pave the way for next-generation treatments that not only enhance immune responses against cancer but also mitigate the immunosuppressive environments often created by tumors. Such advancements could lead to more effective therapies in cancer treatment, significantly improving patient outcomes in oncology. As a result, the study of SIRPA and its recombinant forms stands at the forefront of contemporary immunological research, offering promising avenues for innovative therapeutic interventions.
