Recombinant Human Flt-3 Ligand/FLT3L Protein, CF
Recombinant Human Flt-3 Ligand/FLT3L Protein, CF Summary
Product Specifications
The ED50 for this effect is 0.200-2.00 ng/mL.
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
BT-FT3L
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute the 10 μg size at 100 μg/mL in PBS. Reconstitute all other sizes at 500 μg/mL in PBS |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Scientific Data
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Equivalent bioactivity of GMP (BT-FT3L-GMP), Animal-Free (BT-FT3L-AFL) and RUO (Catalog # BT-FT3L) grades of Recombinant Human Flt-3 Ligand/FLT3L as measured in a cell proliferation assay using OCI-AML5 acute myeloid leukemia cells (orange, green, red, respectively).
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Recombinant Human Flt-3 Ligand/FLT3L Protein (Catalog # BT-FT3L) stimulates cell proliferation of OCI-AML5 acute myeloid leukemia cells. The ED50 for this effect is 0.200‑2.00 ng/mL.
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2 μg/lane of Recombinant Human Flt-3 Ligand/FLT3L Protein (Catalog # BT-FT3L) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 17 kDa, under reducing conditions.
Reconstitution Calculator
Background: Flt-3 Ligand/FLT3L
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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