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 1-3 ng/mL.
Source
E. coli-derived canine SCF/c-kit Ligand protein Lys26-Ala190, with an N-terminal Met
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.1 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
18.5 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.
Publications
Read Publications using 2278-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 under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 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 Canine SCF 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
Canine SCF (stem cell factor; also known as c-kit ligand) is a type I transmembrane (TM) glycoprotein that plays an important role in a number of fetal and adult developmental processes (1 - 4). It is synthesized as a 274 amino acid (aa) precursor that contains a 25 aa signal sequence, a 190 aa extracellular region, a 23 aa TM segment and a 36 aa cytoplasmic tail (5). Within the extracellular region there are four potential N-linked glycosylation sites, two intrachain disulfide bonds, and four alpha -helices. Although the predicted molecular weight is 19 kDa, the native molecule is anywhere from 28 - 40 kDa in size and reflects both N- and O-linked glycosylation (1). Glycosylation is not necessary for bioactivity (6). The transmembrane form of SCF can be cleaved proteolytically, generating a 165 aa soluble form. Circulating SCF exists as both a monomer and nondisulfide-linked homodimer, with monomer predominating (50% to 75%) (6). Both the soluble and TM forms have bioactivity. Their principal targets may be different, however (7). A second, alternate splice short form of SCF has been identified in other species (1). It is membrane bound but lacks the proteolytic cleavage site found in the long form. Thus, it cannot give rise to a soluble molecule. No such isoform has been reported for canine, but it could be assumed to exist. The ratio of long form to short form varies from tissue to tissue (1). Soluble canine SCF shares 88%, 93%, 86%, 83%, 76%, 76%, 86% and 88% aa sequence identity with porcine, feline, bovine, human, mouse, rat, goat and equine SCF, respectively. Cells known to express SCF include endothelial cells, fibroblasts and keratinocytes (1).
Broudy, V.C. (1997) Blood 90:1345.
Nakagawa, S. and T. Kitoh (2000) Curr. Opin. Hematol. 7:133.
Yoshida, H. et al. (2001) J. Invest. Dermatol. Symp. Proc. 6:1.
Kang, J. and S.D. Der (2004) Curr. Opin. Immunol. 16:180.
Dunham, S.P. and D.E. Onions (1996) DNA Seq. 6:233.
The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.
=
÷
Review this Product
Be the first to review our Recombinant Canine SCF Protein, CF and receive a gift card or discount.