Recombinant Human Flt-3 Ligand (Catalog # 308-FKN/CF) stimulates cell proliferation in the BaF3 mouse pro-B cell line transfected with mouse Flt-3. The ED50 for this effect is 0.2-1 ng/mL.
1 µg/lane of Recombinant Human Flt-3 Ligand was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing major bands at24‑28 kDa. Multiple bands are due to variable ...read more
>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
Bioactivity
Theoretical MW
18 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
Multiple bands between 24 kDa and 28 kDa, reducing conditions
Publications
Read Publications using 308-FKN/CF in the following applications:
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.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute 5 µg vials at 50 µg/mL in sterile PBS. Reconstitute 25 µg or larger vials at 100-250 µg/mL in sterile PBS.
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, CF
FL
FLG3L
Flt3 ligand
Flt-3 Ligand
Flt3L
FLT3LG
fms-related tyrosine kinase 3 ligand
SL cytokine
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.
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