Recombinant Human SIRP gamma/CD172g His-tag Protein, CF Summary
Glu29-Pro360, with a C-terminal 6-His tag
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
When Recombinant Human CD47 Fc Chimera (Catalog # 4670-CD) is immobilized at 0.5 µg/mL, Recombinant Human SIRP gamma /CD172g (Catalog #9999-SB) binds with an ED50 of 0.6-3.6 μg/mL.
2 μg/lane of Recombinant Human SIRP gamma /CD172g was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 38-48 kDa.
Background: SIRP gamma/CD172g
Signal regulatory protein gamma (SIRP gamma, designated CD172g), also called SIRP beta 2, is a monomeric 45-47 kDa type I transmembrane protein belonging to the SIRP/SHPS (CD172) family of the Ig superfamily (1-5). SIRP members are "paired receptors" with homology in the extracellular domain but variability in the C‑terminus and signaling function (1, 2). The 387 amino acid (aa) SIRP gamma sequence contains a 28 aa potential signal sequence, a 332 aa extracellular domain (ECD) with four potential N‑glycosylation sites, a 23 aa transmembrane domain and a 4 aa cytoplasmic sequence. SIRP gamma contains one V-type Ig‑like domain that contains a J‑like sequence and two C1-type Ig‑like domains within its ECD (1, 2). Isoforms that lack one (isoform 2, 276 aa) or two (isoform 3, 170 aa) membrane-proximal C‑type Ig-like domains have been described (5). Within the ECD, human SIRP gamma isoform 1 shares 78% aa identity with human SIRP beta 1, and appears to have structurally similar orthologs only in rhesus monkey and chimpanzee (100% and 91% aa identity, respectively) (2). SIRP gamma is the only SIRP known to be expressed on T cells, CD56 bright NK cells and activated NK cells; it is not expressed on myeloid cells (5, 6). It shows adhesion to CD47, but at lower affinity than SIRP alpha (6). Expression of SIRP gamma on T cells suggests a role as an accessory protein interacting with CD47‑expressing antigen presenting cells (5, 6). Unlike SIRP alpha that has cytoplasmic ITIM domains, and SIRP beta 1 that interacts with DAP-12, SIRP gamma does not contain any obvious signaling mechanism (1, 2, 6). However, SIRP gamma -mediated adhesion appears to promote antigen-specific T cell proliferation and co-stimulate T cell activation (5). Engagement of CD47 by SIRP gamma was shown to induce apoptosis on T-cell and monocyte cell lines (6).
- Barclay, A.N. & M.H. Brown (2006) Nat. Rev. Immunol. 6:457.
- vanBeek, E.M. et al. (2005) J. Immunol. 175:7781.
- van den Berg, T.K. et al. (2005) J. Immunol. 175:7788.
- Ichigotani, Y. et al. (2000) J. Hum. Genet. 45:378.
- Piccio, L. et al. (2005) Blood 105:2421.
- Brooke, G. et al. (2004) J. Immunol. 173:2562.
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