Recombinant Human SIRP gamma/CD172g Fc Avi-tag Protein, CF Summary
Additional Information |
Fc Chimera |
Details of Functionality |
Measured by its binding ability in a functional ELISA. Biotinylated
Recombinant Human SIRP gamma /CD172g Fc Chimera Avi-tag (Catalog # AVI4486) binds Recombinant
Human CD47 Fc Chimera (Catalog #
4670-CD) with an ED 50 of 65.0-650 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human SIRP gamma/CD172g protein Human SIRPG (Glu29-Pro360) Accession # Q9P1W8.3 | GGIEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Glu29 |
Structure / Form |
Disulfide-linked homodimer Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
65 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
72-80 kDa, under reducing conditions. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human SIRP gamma/CD172g Fc Avi-tag Protein, CF
Background
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
motif (1, 2, 6). However, SIRP gamma -mediated adhesion appears
to promote antigen-specific T cell proliferation and costimulate T cell
activation (5). Engagement of CD47 by SIRP gamma was shown to induce apoptosis
on T-cell and monocyte cell lines (6). Our Avi-tag Biotinylated Human SIRP gamma Fc Chimera protein features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity
- 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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