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Description
Mouse Anti-Human CD172a (SIRPα) Antibody (S-4039)Product Specification Host Mouse Antigen CD172a (SIRP) Synonyms Tyrosine protein phosphatase non receptor type substrate 1; SHP substrate 1; SHPS 1; Brain Ig like molecule with tyrosine based activation motifs (Bit); CD172 antigen like family member A; Inhibitory receptor SHPS 1; Macrophage fusion receptor; MyD 1 antigen; BIT; MFR; MYD1; PTPNS1; SHPS1; SIRP; SIRPA Location Membrane Accession P78324 Clone Number S 4039 Antibody Type Mouse mAb Isotype
Product Specification
| Host | Mouse |
| Antigen | CD172a (SIRPα) |
| Synonyms | Tyrosine-protein phosphatase non-receptor type substrate 1; SHP substrate 1; SHPS-1; Brain Ig-like molecule with tyrosine-based activation motifs (Bit); CD172 antigen-like family member A; Inhibitory receptor SHPS-1; Macrophage fusion receptor; MyD-1 antigen; BIT; MFR; MYD1; PTPNS1; SHPS1; SIRP; SIRPA |
| Location | Membrane |
| Accession | P78324 |
| Clone Number | S-4039 |
| Antibody Type | Mouse mAb |
| Isotype | IgG2a,k |
| Application | FCM |
| Reactivity | Hu |
| Positive Sample | human peripheral blood leukocytes |
| Purification | Protein A |
| Concentration | 2 mg/ml |
| Conjugation | Unconjugated |
| Physical Appearance | Liquid |
| Storage Buffer | PBS pH7.4 |
| Stability & Storage | 12 months from date of receipt / reconstitution, 2 to 8 °C as supplied |
Dilution
| application | dilution | species |
| FCM | 1:200 | Hu |
Background
Signal-regulatory protein alpha (SIRPα, also known as CD172a or SHPS-1) is a type I transmembrane glycoprotein of the immunoglobulin superfamily, prominently expressed on myeloid cells, neurons, and stem cells, that functions as an inhibitory receptor by binding to the broadly expressed ligand CD47 (the “don’t eat me” signal) to negatively regulate innate immune effector functions such as macrophage phagocytosis of healthy host cells; upon CD47 engagement, phosphorylation of its cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs) recruits phosphatases like SHP-1 and SHP-2, thereby blocking actin cytoskeleton remodeling required for phagocytic activity, while structural studies have revealed its extracellular region contains three Ig-like domains (one V-set and two C1-set) and the interaction surface resembles antigen-receptor binding; in cancer, tumor cells exploit this CD47-SIRPα axis as an innate immune checkpoint to evade phagocytosis, making SIRPα a promising therapeutic target, especially in combination with anti-PD-1/PD-L1 therapies .
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