>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 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
18 kDa, reducing conditions
Publications
Read Publication using 6998-SC 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 with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in 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 Rat SCF Protein
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 rat 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 rat SCF lacks 28 aa that encompasses the primary proteolytic recognition site. Within aa 26 ‑ 189 of the ECD (corresponding to this recombinant protein), rat SCF shares 79% and 94% aa sequence identity with human and mouse 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 (13). SCF assists in the recovery of cardiac function following myocardial infarction by increasing the number of cardiomyocytes and vascular channels (14). In combinantion with G‑CSF, SCF can also reduce the accumulation of beta ‑amyloid deposits in a mouse model of Alzheimer’s disease (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. 88:4671.
Lemmon, M.A. et al. (1997) J. Biol. Chem. 272:6311.
Kanellakis, P. et al. (2006) Cardiovasc. Res. 70:117.
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