Anti-SIRP alpha, clone SAF17.2

Anti-SIRP alpha,, clone SAF17.2, Cat. No. MABS2177, is a mouse monoclonal antibody that detects Tyrosine-protein phosphatase non-receptor type substrate 1 (SIRP alpha) and has been tested for use in Flow Cytometry and Western Blotting.

Flow Cytometry Western Blotting

Western Blotting Analysis: 1 µg/mL from a representative lot detected SIRP alpha in A549 cell lysate.

Western Blotting Analysis: A representative lot detected SIRP alpha in Western Blotting applications (Fournier, B., et. al. (2012). J. Biol. Chem. 287(23); 19386-98).

Flow Cytometry Analysis: A representative lot detected SIRP alpha in Flow Cytometry applications (Lee, W.Y., et. al. (2010). J. Biol. Chem. 285(49); 37953-63).

Clone SAF17.2 is a mouse monoclonal antibody that detects human SIRP alpha protein. It targets an epitope within the extracellular domain.

Eukaryotically expressed SIRP-Fc fusion protein consisting of the extracellular domain.

Stable for 1 year at 2-8°C from date of receipt.

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Evaluated by Western Blotting in U2OS cell lysate.

Western Blotting Analysis: 1 µg/mL of this antibody detected SIRP alpha in U2OS cell lysate.

Tyrosine-protein phosphatase non-receptor type substrate 1 (UniProt: P78324; also known as 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 protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a) is encoded by the SIRPA (also known as BIT, MFR, MYD1, PTPNS1, SHPS1, SIRP) gene (Gene ID: 140885) in human. SIRP alpha is a single-pass type I membrane protein of the Ig superfamily that is ubiquitously expressed with high expression reported in brain. It is also detected on myeloid cells, but not on T cells. SIRP alpha is synthesized with a signal peptide (aa 1-30), which is subsequently cleaved off to generate the mature form that contains an extracellular domain (aa 31-373), a transmembrane domain (aa 374-394) and a cytoplasmic domain (aa 395-504). The extracellular region contains three Ig-like loops. The most distal loop (D1) contains and Ig-like V type domain (aa 32-137) whereas the two membrane proximal loops contain Ig-like C1 type domains (aa 148-247 and 254-348). SIRP alpha serves as an immunoglobulin-like cell surface receptor for CD47 and their interactions is reported to mediate negative regulation of several monocyte/ macrophage functions. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. SIRP alpha also acts as a docking protein and induces translocation of PTPN6, PTPN11, and other binding partners from the cytosol to the plasma membrane. SIRP alpha is phosphorylated on tyrosine residues in response to stimulation with EGF, growth hormone, insulin, and platelet derived growth factor. (Ref.: Lee, WY et al., (2007). J. Immunol.; 179(11); 7741-7750).

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