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Recombinant Human SCF (Mammalian-expressed) Protein, CF Summary
Details of Functionality
Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 1-5 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human SCF/c-kit Ligand protein Glu26-Ala189
>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
Bioactivity
Theoretical MW
18.5 kDa (monomer). 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
24-30 kDa, reducing conditions
Publications
Read Publications using 7466-SC/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 PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 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 SCF (Mammalian-expressed) Protein, CF
c-kit Ligand
DCUA
DFNA69
DKFZp686F2250
familial progressive hyperpigmentation 2
FPH2
FPHH
KIT ligand
Kitl
KITLG
KL-1
Mast cell growth factor
MGF
MGFSHEP7
SCF
SCFStem cell factor
SFc-Kit ligand
SHEP7
SLF
steel factor
Background
Stem cell factor (SCF), also known as c‑kit ligand (KL), mast cell growth factor (MGF), and steel factor (SLF), is a widely expressed 28‑40 kDa type I transmembrane glycoprotein (1). It promotes the survival, differentiation, and mobilization of multiple cell types including myeloid, erythroid, megakaryocytic, lymphoid, germ cell, and melanocyte progenitors (1‑7). SCF is a primary growth and activation factor for mast cells and eosinophils (8). Mature human SCF consists of a 189 amino acid (aa) extracellular domain (ECD), a 23 aa transmembrane segment, and a 36 aa cytoplasmic tail (9). The ECD shows both N‑linked and O‑linked glycosylation (10). Proteolytic cleavage at two alternate sites in the extracellular juxtamembrane region releases a 25 kDa soluble molecule which is comparable to the only form produced by Steel‑dickie mutant mice (11, 12). An alternatively spliced isoform of human SCF exists that lacks 28 aa that encompass the primary proteolytic recognition site (13). Within the ECD of the long isoform (corresponding to this recombinant protein), human SCF shares 79%‑87% aa sequence identity with canine, feline, mouse, and rat SCF. Rat SCF is active on mouse and human cells, but human SCF is only weakly active on mouse cells (9). Noncovalent dimers of transmembrane or soluble SCF interact with the receptor tyrosine kinase SCF R/c‑kit to trigger receptor dimerization and signaling (14). SCF assists in the recovery of cardiac function following myocardial infarction by increasing the number of cardiomyocytes and vascular channels (15).
Ashman, L.K., 1999, Int. J. Biochem. Cell Biol. 31:1037.
Sette, C. et al., 2000, Int. J. Dev. Biol. 44:599.
Yoshida, H. et al., 2001, J. Invest. Dermatol. Symp. Proc. 6:1.
Erlandsson, A. et al., 2004, Exp. Cell Res. 301:201.
Kapur, R. et al., 2002, Blood 100:1287.
Wang, C.-H. et al., 2007, Arterioscler. Thromb. Vasc. Biol. 27:540.
Bashamboo, A. et al., 2006, J. Cell Sci. 119:3039.
Reber, L. et al., 2006, Eur. J. Pharmacol. 533:327.
Martin, F.H. et al., 1990, Cell 63:203.
Arakawa, T. et al., 1991, J. Biol. Chem. 266:18942.
Majumdar, M.K. et al., 1994, J. Biol. Chem. 269:1237.
Brannan, C.I. et al., 1991, Proc. Natl. Acad. Sci. USA 88:4671.
13. Anderson, D.M. et al., 1991, Cell Growth Differ. 2:373.
14. Lemmon, M.A. et al., 1997, J. Biol. Chem. 272:6311.
15. Kanellakis, P. et al., 2006, Cardiovasc. Res. 70:117.
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