SPR with Human SIRP alpha/CD172a Protein 5184

ELISA with Human SIRP alpha/CD172a Protein 5184

Binding assay with Human SIRP alpha/CD172a Protein 5184

Human SIRP alpha/CD172a Protein 5184

$270.00 – $900.00

Summary

Expression: HEK293
Functional: Yes (binding assay)
Amino Acid Range: Glu31-Arg370

SKU: 5184parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P78324
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	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.
molecular weight	The protein has a predicted MW of 38.1 kDa. Due to glycosylation, the protein migrates to 50-65 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human SIRP alpha/CD172a Protein 5184

protein

Size and concentration 100, 500µg and lyophilized
Form 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.
Purity > 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 "donÂ´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
Mass 54967Da
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 Membrane; Single-pass type I membrane protein.
Tissues 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.
Structure 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 N-glycosylated. {ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:9062191}.; 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

Data

SPR with Human SIRP alpha/CD172a Protein

Human SIRP alpha, His Tag captured on Protein A Chip via Anti-His Antibody can bind Human CD47, hFc Tag with an affinity constant of 20.6nM as determined in SPR assay (Biacore T200).

Anti-SIRP alpha Antibody captured on CM5 Chip via Protein A can bind Human Sirpa, His Tag with an affinity constant of 2.81 nM as determined in SPR assay (Biacore T200).

ELISA with Human SIRP alpha/CD172a Protein

Immobilized Human SIRP alpha, His Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Human CD47, hFc Tag with the EC50 of 99.1ng/ml determined by ELISA (QC Test).

Binding assay with Human SIRP alpha/CD172a Protein

Serial dilutions of Anti-SIRP alpha Antibody were added into Human SIRP alpha, His Tag: Biotinylated Human CD47, His Tag binding reactions.The half maximal inhibitory concentration (IC50) is 73.46ng/ml.

The purity of Human SIRP alpha is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human SIRP alpha/CD172a Protein

Human SIRP alpha on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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.