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Biotinylated Human SIRP alpha/CD172a Protein 4767



  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Glu31-Arg370
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-hFc-Avi, also biotinylated

Biotinylated Human SIRP alpha/CD172a Protein 4767

Size and concentration
100, 500µg and lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
> 95% as determined by Tris-Bis PAGE
target relevance
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.
Protein names
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) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (Signal-regulatory prot
Gene names
FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function (By similarity). Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Plays a role in antiviral immunity and limits new world arenavirus infection by decreasing virus internalization (By similarity). Receptor for THBS1 (PubMed:24511121). Interaction with THBS1 stimulates phosphorylation of SIRPA (By similarity). In response to THBS1, involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production (PubMed:24511121). {ECO:0000250, ECO:0000250|UniProtKB:P97710, ECO:0000269|PubMed:10469599, ECO:0000269|PubMed:11509594, ECO:0000269|PubMed:24511121}.
Subellular location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain. Detected on myeloid cells, but not T-cells. Detected at lower levels in heart, placenta, lung, testis, ovary, colon, liver, small intestine, prostate, spleen, kidney, skeletal muscle and pancreas.
SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro. Binds FGR (By similarity). Binds JAK2 irrespective of its phosphorylation status and forms a stable complex. Binds SCAP1 and/or SCAP2. The resulting complex recruits FYB1. Binds PTK2B. Interacts with TRIM2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:18657508, ECO:0000269|PubMed:24511121}.
Post-translational modification
PTM: N-glycosylated. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9062191}.; PTM: Phosphorylated on tyrosine residues in response to stimulation with EGF, growth hormone, insulin and PDGF. Dephosphorylated by PTPN11. {ECO:0000269|PubMed:10842184, ECO:0000269|PubMed:9062191}.
Target Relevance information above includes information from UniProt accession : P78324
The UniProt Consortium


ELISA with Biotinylated Human SIRP alpha/CD172a Protein
Immobilized Human CD47, His Tag at 2µg/ml (100µl/Well) on the plate. Dose response curve for Biotinylated Human SIRP alpha, hFc Tag with the EC50 of 0.22µg/ml determined by ELISA.
HPLC of Biotinylated Human SIRP alpha CD172a Protein
The purity of Biotinylated Human SIRP alpha is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated Human SIRP alpha CD172a Protein
Biotinylated Human SIRP alpha on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.


Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.



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