Recombinant Human SIRP gamma/CD172g His Avi-tag Protein, CF Summary
Additional Information |
Biotinylated His-tag |
Details of Functionality |
Measured by its binding ability in a functional ELISA. Biotinylated
Recombinant Human SIRP gamma /CD172g His-tag Avi-tag (Catalog # AVI9999) binds Recombinant
Human CD47 Fc Chimera (Catalog #
4670-CD)
with an ED 50 of 0.150-3.00
μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human SIRP gamma/CD172g protein Human SIRPG (Glu29-Pro360) Accession # Q9P1W8.3 | 6-His tag | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Glu29 |
Structure / Form |
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 |
39 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 |
42-49 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 250 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 His 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, CD56bright 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 (5-7). 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
Recombinant Human SIRP gamma /CD172g His-tag 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.
- Smith, M.J. et al. (2022)
Diabetes. 71:350.
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