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NCGC00138783 TFA is a selective inhibitor targeting CD47/SIRPα axis, with an IC50 of 50 μM. NCGC00138783 TFA directly blocks the interaction between CD47 and SIRPα axis .
NCGC00138783 is a selective inhibitor targeting CD47/SIRPα axis, with an IC50 of 50 µM. NCGC00138783 directly blocks the interaction between CD47 and SIRPα axis .
DMUP is a potent CD47-SIRPα axis inhibitor. DMUP induces apoptosis and increases the macrophage phagocytosis in A549 cells. DMUP decreases the expression of CD47 and SIRPα protein. DMUP shows antitumor activity .
NCGC00138783 free base is a selective inhibitor targeting CD47/SIRPα axis, with an IC50 of 50 µM. NCGC00138783 free base directly blocks the interaction between CD47 and SIRPα axis .
Glutaminyl cyclases-IN-1 (IsoQC-IN-1) is a potent glutaminyl cyclases (QC) inhibitor with IC50 values of 12 nM and 73 nM for human QC and isoQC, respectively. Glutaminyl cyclases-IN-1 can selectively interfere with the interaction of CD47/SIRPα through isoQC inhibition, and enhances the increased phagocytic activity of both THP-1 and U937 macrophages .
RS17 is an anti-tumor peptide designed to bind specifically to the CD47 molecule and block the interaction between CD47 and its ligand, SIRPα, on the surface membrane of macrophages. The main regulatory mechanism of RS17 is to prevent CD47 from transmitting selective phagocytosis signals to SIRPα by binding to CD47, so that macrophages do not recognize tumor cells as their own tissue, but phagocytose them as foreign substances, thereby inhibiting immune escape of tumor cells. RS17 can be used to study the mechanism of anti-tumor response and immune escape .
RRx-001, a hypoxia-selective epigenetic agent and studied as a radio- and chem-sensitizer, triggers apoptosis and overcomes agent resistance in myeloma. RRx-001 exhibits potent anti-tumor activity with minimal toxicity . RRx-001 is a dual small molecule checkpoint inhibitor by downregulating CD47 and SIRP-α . RRx-001 is a potent inhibitor of G6PD and shows potent antimalarial activity .
RS17 is an anti-tumor peptide designed to bind specifically to the CD47 molecule and block the interaction between CD47 and its ligand, SIRPα, on the surface membrane of macrophages. The main regulatory mechanism of RS17 is to prevent CD47 from transmitting selective phagocytosis signals to SIRPα by binding to CD47, so that macrophages do not recognize tumor cells as their own tissue, but phagocytose them as foreign substances, thereby inhibiting immune escape of tumor cells. RS17 can be used to study the mechanism of anti-tumor response and immune escape .
KWAR23 is an anti-human SIRPα antibody. KWAR23 binds human SIRPα with high affinity and disrupts its binding to CD47. KWAR23 shows antitumor activity in combination with tumor-opsonizing antibodies and can be used in cancer immunotherapy research .
Anzurstobart (CC-95251; BMS-986351) is a high-affinity, fully human monoclonal anti-SIRPα antibody that blocks the binding of CD47 to SIRPα. Anzurstobart enhances macrophage phagocytic activity against DLBCL cell lines in co-culture models when combined with the antibody Rituximab (HY-P9913). Anzurstobart has the potential for solid and hematologic malignancies research .
Letaplimab (IBI-188) is a human IgG4 anti-CD47 monoclonal antibody. CD47 is overexpressed on cancer cells, it is a ligand for SIRPα. Letaplimab enhances tumor cell phagocytosis .
Ontorpacept (TTI-621) is a soluble fusion protein that consists of the human SIRPα N-terminal (1-118) linked to the Fc region of human IgG1. The N-terminal (1-118)-fragment of ontorpacept is a binding domain for CD47 which is an inhibitor of phagocytosis by macrophages. Ontorpacept is a CD47-blocking checkpoint inhibitor with antitumor activity .
The SIRP α/CD172a protein is an immunoglobulin-like cell surface receptor for CD47 and is essential for the translocation of binding partners to the plasma membrane. It plays a key role in a variety of cellular processes, supporting the adhesion of cerebellar neurons, promoting neurite outgrowth, and promoting glial cell attachment. SIRP alpha/CD172a Protein, Mouse (HEK293, His) is the recombinant mouse-derived SIRP alpha/CD172a protein, expressed by HEK293 , with C-6*His labeled tag. The total length of SIRP alpha/CD172a Protein, Mouse (HEK293, His) is 342 a.a., with molecular weight of 60-110 kDa.
SIRP-beta (Sirpb, CD172b) is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins, Sirpb was found to interact with TYROBP/DAP12, a transmembrane adaptor protein bearing immunoreceptor tyrosine-based activation motifs, resulting in the tyrosine phosphorylation of DAP12 and the subsequent recruitment of Syk to the Sirpb-DAP12 complex. Sirpb is also implicated as a positive regulator of hematopoietic cells. SIRP beta Protein, Mouse (HEK293, His) is the recombinant mouse-derived SIRP beta protein, expressed by HEK293 , with C-His labeled tag.
SIRP γ protein is a possible immunoglobulin-like cell surface receptor that mediates cell-cell adhesion by binding to CD47. This interaction enhances antigen-specific T cell proliferation and provides costimulatory signals for T cell activation, highlighting the role of SIRP gamma in regulating immune responses. SIRP gamma Protein, Human (HEK293, His-Avi) is the recombinant human-derived SIRP gamma protein, expressed by HEK293 , with C-His, C-Avi labeled tag.
SIRP γ protein is a possible immunoglobulin-like cell surface receptor that mediates cell-cell adhesion by binding to CD47. This interaction enhances antigen-specific T cell proliferation and provides costimulatory signals for T cell activation, highlighting the role of SIRP gamma in regulating immune responses. SIRP gamma Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived SIRP gamma protein, expressed by HEK293 , with C-His, C-Avi labeled tag.
When paired with KLRD1, the NKG2C/CD159c protein recognizes MHC-E loaded with MHC-G peptides, thereby contributing to NK cell generation and function. It also regulates cytotoxic lymphocytes in viral infections. SIRP alpha/CD172a Protein, Rat (HEK293, Fc) is the recombinant rat-derived SIRP alpha/CD172a protein, expressed by HEK293 , with C-hFc labeled tag. The total length of SIRP alpha/CD172a Protein, Rat (HEK293, Fc) is 373 a.a., with molecular weight of ~64.25 kDa.
When paired with KLRD1, the NKG2C/CD159c protein recognizes MHC-E loaded with MHC-G peptides, thereby contributing to NK cell generation and function. It also regulates cytotoxic lymphocytes in viral infections. SIRP alpha/CD172a Protein, Rat (HEK293, His) is the recombinant rat-derived SIRP alpha/CD172a protein, expressed by HEK293 , with C-His labeled tag. The total length of SIRP alpha/CD172a Protein, Rat (HEK293, His) is 342 a.a., with molecular weight of 63-80 kDa.
The SIRP α/CD172a protein is an immunoglobulin-like cell surface receptor for CD47 and is essential for the translocation of binding partners to the plasma membrane. It plays a key role in a variety of cellular processes, supporting the adhesion of cerebellar neurons, promoting neurite outgrowth, and promoting glial cell attachment. SIRP alpha/CD172a Protein, Mouse (BAA20376, HEK293, Fc) is the recombinant mouse-derived SIRP alpha/CD172a protein, expressed by HEK293 , with C-hFc labeled tag. The total length of SIRP alpha/CD172a Protein, Mouse (BAA20376, HEK293, Fc) is 342 a.a., with molecular weight of approximately 100-120 kDa.
Signal-Regulatory protein Gamma; sirp-Gamma; cd172 Antigen-Like Family Member B; Signal-Fegulatory protein Beta-2; sirp-b2; sirp-Beta-2; cd172g; sirpG; sirpB2
SIRP γ protein is a possible immunoglobulin-like cell surface receptor that mediates cell-cell adhesion by binding to CD47. This interaction enhances antigen-specific T cell proliferation and provides costimulatory signals for T cell activation, highlighting the role of SIRP gamma in regulating immune responses. SIRP gamma Protein, Human (HEK293, Fc) is the recombinant human-derived SIRP gamma protein, expressed by HEK293 , with C-hFc labeled tag.
The SIRP α/CD172a protein is an immunoglobulin-like cell surface receptor for CD47 and is essential for the translocation of binding partners to the plasma membrane. It plays a key role in a variety of cellular processes, supporting the adhesion of cerebellar neurons, promoting neurite outgrowth, and promoting glial cell attachment. SIRP alpha/CD172a Protein, Cynomolgus (339a.a, HEK293, His) is the recombinant cynomolgus-derived SIRP alpha/CD172a protein, expressed by HEK293 , with C-6*His labeled tag. The total length of SIRP alpha/CD172a Protein, Cynomolgus (339a.a, HEK293, His) is 339 a.a., with molecular weight of 52-70 kDa.
SIRP beta 1 protein negatively regulates receptor tyrosine kinase signaling and recruits SYK for myeloid cell activation. It interacts with TYROBP as a homodimer, facilitating SYK recruitment. This intricate molecular interplay is crucial for modulating myeloid cell activation and regulating cellular signaling. SIRP beta 1 occupies a central position in protein interactions that contribute to its functional role. SIRP Beta 1 Protein, Human (HEK293, His-Avi) is the recombinant human-derived SIRP Beta 1 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of SIRP Beta 1 Protein, Human (HEK293, His-Avi) is 340 a.a., with molecular weight of 52-60 kDa.
SIRP beta 1 protein negatively regulates receptor tyrosine kinase signaling and recruits SYK for myeloid cell activation. It interacts with TYROBP as a homodimer, facilitating SYK recruitment. This intricate molecular interplay is crucial for modulating myeloid cell activation and regulating cellular signaling. SIRP beta 1 occupies a central position in protein interactions that contribute to its functional role. SIRP Beta 1 Protein, Human (Biotinylated, HEK293, C-His-Avi) is the recombinant human-derived SIRP Beta 1 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of SIRP Beta 1 Protein, Human (Biotinylated, HEK293, C-His-Avi) is 340 a.a., with molecular weight of 55-65 kDa.
SIRP gamma Protein, a member of signal-regulatory protein (SIRP) family, is the only SIRP detected on T cells and activated NK cells. SIRP gamma can bind CD47, providing T cells and NK cells with a cell surface molecule capable of interacting with CD47. SIRP gamma-CD47 interaction mediates strong cell-cell adhesion and supports T cell-APC contact, enhancing antigen presentation and consequent T-cell proliferation and cytokine secretion. SIRP gamma Protein, Cynomolgus (HEK293, Fc) is the recombinant cynomolgus-derived SIRP gamma protein, expressed by HEK293 , with C-hFc labeled tag.
SIRP gamma Protein, a member of signal-regulatory protein (SIRP) family, is the only SIRP detected on T cells and activated NK cells. SIRP gamma can bind CD47, providing T cells and NK cells with a cell surface molecule capable of interacting with CD47. SIRP gamma-CD47 interaction mediates strong cell-cell adhesion and supports T cell-APC contact, enhancing antigen presentation and consequent T-cell proliferation and cytokine secretion. SIRP gamma Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived SIRP gamma protein, expressed by HEK293 , with C-His labeled tag.
SIRP Beta 1 Protein, an immunoglobulin-like cell surface receptor, crucially negatively regulates receptor tyrosine kinase-coupled signaling processes. It modulates cellular responses to stimuli like cell adhesion, growth factors, or insulin, contributing to maintaining cellular homeostasis and finely tuning signaling pathways associated with receptor tyrosine kinases. SIRP Beta 1 Protein, Human (isoform 3, HEK293, His-Avi) is the recombinant human-derived SIRP Beta 1 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of SIRP Beta 1 Protein, Human (isoform 3, HEK293, His-Avi) is 342 a.a., with molecular weight of 60-70 kDa.
SIRP Beta 1 Protein, an immunoglobulin-like cell surface receptor, crucially negatively regulates receptor tyrosine kinase-coupled signaling processes. It modulates cellular responses to stimuli like cell adhesion, growth factors, or insulin, contributing to maintaining cellular homeostasis and finely tuning signaling pathways associated with receptor tyrosine kinases. SIRP Beta 1 Protein, Human (Biotinylated, isoform 3, HEK293, His-Avi) is the recombinant human-derived SIRP Beta 1 protein, expressed by HEK293 , with C-His, C-Avi labeled tag. The total length of SIRP Beta 1 Protein, Human (Biotinylated, isoform 3, HEK293, His-Avi) is 342 a.a., with molecular weight of 55-68 kDa.
SIRP beta 2 Protein, a novel positive regulator of innate immunotherapy, is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP beta 2 is expressed on myeloid cells at protein level and enhanced adhesion, differentiation, cancer cell phagocytosis and T cell activation in an in vitro setting. DAP12 is responsible for SIRP beta 2 signaling, and is recruited through a single, positive lysine residue in the transmembrane domain of SIRP beta 2. SIRP beta 2 Protein, Human (HEK293, Fc) is the recombinant human-derived SIRP beta 2 protein, expressed by HEK293 , with C-hFc labeled tag.
SIRP beta 1 protein negatively regulates receptor tyrosine kinase signaling and recruits SYK for myeloid cell activation. It interacts with TYROBP as a homodimer, facilitating SYK recruitment. This intricate molecular interplay is crucial for modulating myeloid cell activation and regulating cellular signaling. SIRP beta 1 occupies a central position in protein interactions that contribute to its functional role. SIRP beta 1 Protein, Human (HEK293, His) is the recombinant human-derived SIRP beta 1 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of SIRP beta 1 Protein, Human (HEK293, His) is 333 a.a., with molecular weight of 45-55 kDa.
SIRP beta 1 protein negatively regulates receptor tyrosine kinase signaling and recruits SYK for myeloid cell activation. It interacts with TYROBP as a homodimer, facilitating SYK recruitment. This intricate molecular interplay is crucial for modulating myeloid cell activation and regulating cellular signaling. SIRP beta 1 occupies a central position in protein interactions that contribute to its functional role. SIRP beta 1 Protein, Human (HEK293, His-Myc) is the recombinant human-derived SIRP beta 1 protein, expressed by HEK293 , with N-6*His, N-Myc labeled tag. The total length of SIRP beta 1 Protein, Human (HEK293, His-Myc) is 342 a.a., with molecular weight of 41.3 kDa.
SIRP alpha/CD172a Protein, Human (CAA71403.1, HEK 293, Fc) is a recombinant protein expressed in HEK 293 cells. SIRP alpha/CD172a Protein, Human (CAA71403.1, HEK 293, Fc) is expressed with the Fc region of mouse IgG2a at the C-terminus.
The SIRP α/CD172a protein is an immunoglobulin-like cell surface receptor for CD47 and is essential for the translocation of binding partners to the plasma membrane. It plays a key role in a variety of cellular processes, supporting the adhesion of cerebellar neurons, promoting neurite outgrowth, and promoting glial cell attachment. SIRP alpha/CD172a Protein, Cynomolgus (Biotinylated, HEK293, His-Avi) is the recombinant cynomolgus-derived SIRP alpha/CD172a protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of SIRP alpha/CD172a Protein, Cynomolgus (Biotinylated, HEK293, His-Avi) is 340 a.a., with molecular weight of 66 kDa.
SIRP alpha/CD172a Protein, Human (CAA71403.1, HEK 293, His)
, as a recombinant protein produced in HEK293 cells, is a polypeptide chain with a His tag.
sirpA; BIT; MFR; MYD1; PTPNS1; SHPS1; sirp; 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; Inhibito
WB, FC
Human
SIRP alpha Antibody (YA1361) is a rabbit-derived non-conjugated IgG antibody (Clone NO.: YA1361), targeting SIRP alpha. SIRP alpha Antibody (YA1361) can be used for FC,WB experiment in human background.
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