Recombinant Human VSIG4 Fc Chimera Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
The biotin to protein ratio is greater than 0.7 as determined by the HABA assay. Measured by its binding ability in a functional ELISA. When Human iC3b is Immobilized at 2.5 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human VSIG4 Fc Chimera Avi‑tag (AVI4646) that produces 50% optimal binding response is found to be approximately 5-40 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human VSIG4 protein Human VSIG4 (Arg20-Pro283) Accession # Q9Y279.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | |
|
Accession # |
|
N-terminal Sequence |
Arg20 |
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 |
58 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 |
65-85 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 200 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 VSIG4 Fc Chimera Avi-tag Protein, CF
Background
V-set and immunoglobulin domain containing 4 (VSIG4), also
known as CRIg and Z39IG, is a type I transmembrane protein of the B7 family and
complement receptor of the immunoglobulin superfamily. Human VSIG4 consists
of an extracellular domain (ECD) containing a V-type and a C2-type Ig domain, a
transmembrane domain and a cytoplasmic domain (3). Interestingly, VISG4 in
several animals, including mouse and rat, lack the C2-type Ig domain present in
human VSIG4. Within the IgV domain, mature human VSIG4 shares 80% and 78% amino
acid identity with mouse and rat VSIG4, respectively. Alternative splicing results in numerous isoforms
lacking all or part of the cytoplasmic domain, the C2-type Ig domain and/or the
transmembrane domain. VSIG4 is specifically expressed on macrophages in the
thymic medulla, peritoneum, alveoli, synovia, adipose and heart, liver Kupffer
cells, placental Hofbauer cells, and atherosclerotic foam cells (1-8). It is
absent on infiltrating macrophages (8). VSIG4 is a complement receptor that
binds C3b and iC3b fragments, internalizes them to recycling endosomes, and is
recycled to the cell surface (4, 5). It contributes significantly to innate
immunity by binding and phagocytosis of complement-opsonized invading pathogens
(4, 7, 9). Binding of either native or recombinant soluble VSIG4 to C3b
inhibits complement amplification through the alternative, but not classical,
pathway (9, 10). VSIG4 is also a negative regulator of mouse and human T cell
activation (2). Although VSIG4 engagement may activate NF kappa B and thus be
pro-inflammatory in some cases, many of its activities are important in
resolving, rather than initiating, inflammation (1, 2, 6, 9, 10). VSIG4
expression has been implicated in lung cancer development and associated with
poor prognosis of high grade glioma (11, 12). Our Avi-tag Biotinylated
Recombinant VSIG4 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.
- 1. He, J.Q. et al. (2008) Mol. Immunol. 4041.
- Vogt, L. et al. (2006) J. Clin. Invest. 116:2817.
- Langnaese, K. et al. (2000) Biochim. Biophys. Acta 1492:522.
- Helmy, K. et al. (2006) Cell 124:915.
- Tanaka, M. et al. (2008) Clin. Exp. Immunol. 154:38.
- Lee, M-Y. et al. (2006) J. Leukoc. Biol. 80:922.
- Gorgani, N.N. et al. (2008) J. Immunol. 181:7902.
- Walker, M.G. (2002) Biochim. Biophys. Acta 1574:387.
- Wiesmann, C. et al. (2006) Nature 444:217.
- Katschke, K.J. et al. (2007) J. Exp. Med. 204:1319.
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