Recombinant Human Flt-3 Ligand/FLT3L Protein Summary
Details of Functionality |
Measured in a cell proliferation assay using BaF3 mouse pro‑B cells transfected with mouse Flt-3. The ED50 for this effect is 0.200-1.00 ng/mL. |
Source |
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Flt-3 Ligand/FLT3L protein Thr27-Pro185 |
Accession # |
|
N-terminal Sequence |
Thr27 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
FLT3LG |
Purity |
>97%, 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 |
17.5 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 |
17-30 kDa, reducing conditions |
Publications |
Read Publications using 308-FK in the following applications:
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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 Acetonitrile and TFA with BSA as a carrier protein. |
Purity |
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Flt-3 Ligand/FLT3L Protein
Background
Flt‑3 Ligand, also known as FLT3L, is an alpha-helical cytokine that promotes the differentiation of multiple hematopoietic cell lineages (1-3). Mature human Flt‑3 Ligand consists of a 158 amino acid (aa) extracellular domain (ECD) with a cytokine-like domain and a juxtamembrane tether region, a 21 aa transmembrane segment, and a 30 aa cytoplasmic tail (4-7). Within the ECD, human Flt‑3 Ligand shares 71% and 65% aa sequence identity with mouse and rat Flt‑3 Ligand, respectively (4-6). The human and mouse Flt‑3 Ligand proteins show cross-species activity. Flt-3 Ligand is also structurally related to M-CSF and SCF. Flt-3 Ligand is widely expressed in various human and mouse tissues. It is expressed as a noncovalently-linked dimer by T cells and bone marrow and thymic fibroblasts (1, 8). Each 36 kDa chain of the Flt-3 Ligand dimer carries approximately 12 kDa of N- and O-linked carbohydrates (8). Alternate splicing and proteolytic cleavage of the transmembrane form of the Flt-3 Ligand protein can generate a soluble 30 kDa fragment that includes the cytokine-like domain (4, 8). Alternate splicing of human Flt‑3 Ligand also generates membrane-associated isoforms that contain either a truncated cytoplasmic tail or an 85 aa substitution following the cytokine-like domain in the ECD of the Flt-3 Ligand protein (4, 5, 8). Both transmembrane and soluble forms of Flt‑3 Ligand signal through the tyrosine kinase receptor Flt-3/Flk-2 (3, 4, 6, 7). Flt‑3 Ligand induces the expansion of monocytes and immature dendritic cells as well as early B cell lineage differentiation (2, 9). Additionally, Flt-3 Ligand synergizes with IL-3, GM-CSF, and SCF to promote the mobilization and myeloid differentiation of hematopoietic stem cells (4-6). Flt-3 Ligand also cooperates with IL-2, IL-6, IL-7, and IL-15 to induce NK cell development and with IL-3, IL-7, and IL-11 to induce terminal B cell maturation (1, 10). Animal studies show that Flt‑3 Ligand reduces the severity of experimentally induced allergic inflammation (11).
- Wodnar-Filipowicz, A. (2003) News Physiol. Sci. 18:247.
- Dong, J. et al. (2002) Cancer Biol. Ther. 1:486.
- Gilliland, D.G. and J.D. Griffin (2002) Blood 100:1532.
- Hannum, C. et al. (1994) Nature 368:643.
- Lyman, S.D. et al. (1994) Blood 83:2795.
- Lyman, S.D. et al. (1993) Cell 75:1157.
- Savvides, S.N. et al. (2000) Nat. Struct. Biol. 7:486.
- McClanahan, T. et al. (1996) Blood 88:3371.
- Diener, K.R. et al. (2008) Exp. Hematol. 36:51.
- Farag, S.S. and M.A. Caligiuri (2006) Blood Rev. 20:123.
- Edwan, J.H. et al. (2004) J. Immunol. 172:5016.
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