SIRP AlphaV2 protein (His tag)
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- Target
- SIRP AlphaV2
- Protein-Typ
- Recombinant
- Spezies
- Human
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Quelle
- HEK-293 Cells
- Aufreinigungstag / Konjugat
- His tag
- Sequenz
- Glu31-Arg369
- Reinheit
- > 95% as determined by Tris-Bis PAGE,> 95% as determined by HPLC
- Sterilität
- 0.22 μm filtered
- Endotoxin-Niveau
- Less than 1EU per μg by the LAL method.
- Biological Activity Comment
- Immobilized Human SIRP alpha V2, His Tag at 1μg/ml (100μl/Well) on the plate. Dose response curve for Human CD47, hFc Tag with the EC50 of 0.15μg/ml determined by ELISA. The affinity constant of 9.11nM as determined in SPR assay (Biacore T200). See testing image for detail.
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- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Lyophilized
- Rekonstitution
- Centrifuge tubes before opening. Reconstituting to a concentration more than 100 μg/mL is recommended (usually we use 1 mg/mL solution for lyophilization). Dissolve the lyophilized protein in distilled water.
- Buffer
- Lyophilized from 0.22μm filtered solution in PBS ( pH 7.4). Normally 5 % trehalose is added as protectant before lyophilization.
- Lagerung
- 4 °C,-80 °C
- Informationen zur Lagerung
- Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- Haltbarkeit
- 12 months
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- Target
- SIRP AlphaV2
- Andere Bezeichnung
- SIRP alpha V2
- Hintergrund
- CD172a, BIT, MFR, MYD1, MYD-1, P84, PTPNS1, SHP substrate 1, SHPS1, SHPS-1, SHPS1CD172A, SIRP alpha, SIRPA, Sirp-alpha-1, SIRPalpha2, Sirp-alpha-2, Sirp-alpha-3,Signal regulatory protein α (SIRPα) is a regulatory membrane glycoprotein from SIRP family expressed mainly by myeloid cells and also by stem cells or neurons.SIRPα acts as inhibitory receptor and interacts with a broadly expressed transmembrane protein CD47 also called the "don´t eat me" signal.Cancer cells highly expressed CD47 that activate SIRP α and inhibit macrophage-mediated destruction.
- Molekulargewicht
- 38 kDa. Due to glycosylation, the protein migrates to 55-65 kDa based on Tris-Bis PAGE result.
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