Recombinant Human SIRPA Protein (C-6His)

Name: Recombinant Human SIRPA Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-2546NP
Availability: InStock

BL-2546NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, Cluster of differentiation (cd) proteins, Co-inhibitory receptors, Featured cd protein molecules, Featured immune checkpoint protein molecules, High-quality recombinant proteins, Immune checkpoint proteins

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Product Overview

Description	Recombinant Human Signal-Regulatory Protein Alpha 1 is produced by our Mammalian expression system and the target gene encoding Glu31-Arg370 is expressed with a 6His tag at the C-terminus.
Accession	P78324
Synonym	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 Feceptor SHPS-1; Macrophage Fusion Receptor; MyD-1 Antigen; Signal-Regulatory Protein Alpha-1; Sirp-Alpha-1; Signal-Regulatory Protein Alpha-2; Sirp-Alpha-2; Signal-Regulatory Protein Alpha-3; Sirp-Alpha-3; p84; CD172a; SIRPA; BIT; MFR; MYD1; PTPNS1; SHPS1; SIRP
Gene Background	Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation
Molecular Mass	38.1 KDa
Apmol Mass	45-60 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Biologically active. Please contact us to obtain bioactivity data.
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target 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. 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.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Database References	HGNC: 9662 OMIM: 602461 KEGG: hsa:140885 STRING: 9606.ENSP00000348307 UniGene: PMID: 28669759 SIRP alpha protein is under-expressed in low and high-grades of astrocytoma from patients' brain samples. PMID: 27900675 Anti-SIRPA antibody immunotherapy enhances neutrophil and macrophage antitumor activity. PMID: 29158380 SIRPalpha might play an important role in the progression of oral leukoplakia and oral cancer, and could be a pivotal therapeutic target in oral squamous cell carcinoma, regulating the phenotype of macrophages via targeting NF-kappaB signaling. PMID: 27793032 TTI-621 (SIRPalphaFc) is a fully human recombinant fusion protein that blocks the CD47-SIRPalpha axis by binding to human CD47 and enhancing phagocytosis of malignant cells..These data indicate that TTI-621 is active across a broad range of human tumors. PMID: 27856600 data suggest that TTI-621 may be efficacious in triggering the destruction of cancer cells by a diverse population of TAMs found in vivo and support possible combination approaches to augment the activity of CD47 blockade PMID: 29084248 CD47, TSP1, and to a lesser extent SIRPalpha facilitate exosome-mediated myeloid-derived suppressor cells chemotaxis and migration. PMID: 27728760 exploited by Hepatitis E virus to negative regulated IFN-beta of the host innate immune system to promote viral infection PMID: 26492885 Data suggest a reduction in the CD47 antigen/signal-regulatory protein alpha (SIRPalpha) pathway by programmed cell death protein 1 (PD-1) blockade, which regulates Myeloid-derived suppressor cells (MDSCs) and tumor associated macrophages (TAMs). PMID: 26573233 agents that block the CD47:SIRP-alpha engagement are attractive therapeutic targets as a monotherapy or in combination with additional immune-modulating agents for activating antitumor T cells in vivo PMID: 26116271 the data suggest that combinatorial actions of ADAM10 and gamma-secretase on SIRPalpha cleavage promote inflammatory signaling. PMID: 26534964 Loss of cell surface CD47 clustering formation and binding avidity to SIRPalpha facilitate apoptotic cell clearance by macrophages. PMID: 26085683 Velcro" engineering of high affinity CD47 ectodomain as signal regulatory protein alpha (SIRPalpha) antagonists that enhance antibody-dependent cellular phagocytosis PMID: 25837251 negatively regulates neutrophil accumulation during inflammation PMID: 24516072 Combinatorial expression of NKX2-5, SIRPA, VCAM1 and CD34 can be used to define discrete stages of cardiovascular cell lineage differentiation. PMID: 24968096 These results suggest that thrombospondin-1 binding to SIRP-alpha on nonphagocytic cells activates NADPH oxidase, limits vasodilation, and promotes renal ischemia reperfusion injury. PMID: 24511121 'clustering' SIRPalpha into plasma membrane microdomains is essential for activated monocytes and macrophages to effectively interact with CD47 and initiate intracellular signaling PMID: 24143245 Polymorphisms in the human inhibitory signal-regulatory protein alpha do not affect binding to its ligand CD47. PMID: 24550402 SIRPA plays a protective role in cardiac hypertrophy through negative regulation of the Toll-like receptor 4/nuclear factor-kappaB pathway. PMID: 24101669 These results demonstrate a SIRPalpha-based mechanism that dynamically regulates polymorphonuclear leukocyte inflammatory responses. PMID: 24026300 Signal regulatory protein alpha is associated with tumor-polarized macrophages phenotype switch and plays a pivotal role in tumor progression. PMID: 23504854 An avidity-improved CD47 fusion protein (CD47-Var1) suppresses the release of a wide array of inflammatory cytokines by CD172a(+) cells. PMID: 23669395 Expression of SIRPalpha on two low SIRPalpha acute myeloid leukemia (AML) expressing cell lines could be upregulated upon differentiation of the cells. PMID: 23320069 SHPS-1 negatively regulates the MyD88-dependent TLR signaling pathway through the inhibition of NF-kappaB activation PMID: 23314616 IFN-beta and IFN-gamma/TNF-alpha decrease erythrophagocytosis by human monocytes in vitro, and this effect does not apparently require an increase in SIRP-alpha or SHP-1 expression. PMID: 22738830 neutrophils reduce their SIRPalpha expression during apoptosis, which may be part of the functional down-regulation seen in apoptotic neutrophils. PMID: 23271705 thymic Sirpalpha(+) cDCs crucially contribute to a process of intrathymic tumor immune tolerance that involves CCR2 and CCL2 PMID: 22815949 In the glomeruli of CNS patients carrying mutations in NPHS1, where SD formation is disrupted, the expression of SIRPalpha as well as Neph1 and nephrin was significantly decreased, indicating that SIRPalpha is closely associated with the nephrin complex PMID: 22747997 Surfactant protein D (Sp-D) binds to membrane-proximal domain (D3) of signal regulatory protein alpha (SIRPalpha), a site distant from binding domain of CD47, while also binding to analogous region on signal regulatory protein beta (SIRPbeta). PMID: 22511785 SIRPalpha1 in hepatic sinusoid Kupffer cells is associated with the extent of autoimmune hepatitis. PMID: 22409853 data, taken together with similar findings with other human neoplasms, show that CD47 is a commonly expressed molecule on all cancers, its function to block phagocytosis is known, and blockade of its function leads to tumor phagocytosis and elimination PMID: 22451913 SIRPalpha/CD172a and FHOD1 are unique markers of littoral cells, a recently evolved major cell population of red pulp of human spleen. PMID: 22490440 Sensing of cell surface CD47 expression by phagocyte SIRPalpha is a critical determinant of T- and natural killer-cell homeostasis under steady-state conditions in vivo. PMID: 21788504 hSIRPa-transgenic Rag2(-/-)gamma(c)(-/-) mice represent a unique mouse strain supporting high levels of human cell engraftment. PMID: 21788509 The prolactin receptor (PRLr)-SIRPalpha-integrin complex provides a basis for integrin-PRLr cross-talk that contributes to the biology of breast cancer. PMID: 20826546 the relationships between SIRPalpha1 and beta-catenin in leukemia cells. PMID: 21369691 Single Nucleotide Polymorphisms in PTPNS1 is associated with inflammatory bowel disease. PMID: 21225905 SHP-2 as an essential component of tumor suppression and anoikis mediated by SIRPalpha1 in human breast carcinoma cells as well as in v-Src-transformed cells. PMID: 21169408 Poor prognosis of breast cancer patients with high expression of CD47 is due to an active CD47/SIRPA signaling pathway in circulating cells. PMID: 20705613 The role of cis dimerization of signal regulatory protein alpha (SIRPalpha) in binding to CD47. PMID: 20826801 Findings reveal a novel mechanism for recruitment of PDK1 to the SHPS-1 signaling complex, which is required for IGF-I-stimulated AKT Thr(308) phosphorylation and inhibition of apoptosis. PMID: 20643654 Inhibition of engulfment correlates with affinity of CD47 for SIRPA - but only at low levels of CD47. PMID: 20299253 SIRPalpha1 specifically affects the SHP-2/FAK/Grb2/Sos-1/MAPK activation loop to downmodulate EGFRvIII-mediated migration and transformation. PMID: 20473329 Insulin-like growth factor-I-stimulated insulin receptor substrate-1 negatively regulates Src homology 2 domain-containing protein-tyrosine phosphatase substrate-1 function in vascular smooth muscle cells. PMID: 20207740 SIRP alpha gene expression is higher in monocytes from autoimmune hemolytic anemia patients, compared with basal expression. PMID: 19874234 CD47/SIRP-alpha interactions are implicated in the pathogenesis of DC-driven allergic airway inflammation. PMID: 19748659 Signal regulatory protein (SIRPalpha), a cellular ligand for CD47, regulates neutrophil transmigration PMID: 11792697 The interaction of SHPS-1 with CD47 may contribute to the recruitment of B lymphocytes via endothelial cells under steady state conditions. PMID: 11907074 MyD-1-coupling to this PI 3-kinase-dependent signaling pathway may therefore present a novel target for the development of therapeutic strategies for combating TNFalpha production and consequent inflammatory disease. PMID: 12805067 Expression of SIRPalpha1 on astrocytomas may be of considerable importance in brain tumor biology. PMID: 14729615

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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