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Recombinant Human SCF Protein, CF

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Recombinant Human SCF Protein (Catalog # BT-SCF) has a molecular weight (MW) of 42.1 kDa as analyzed by SEC-MALS, suggesting that this protein is a homodimer. 
Recombinant Human SCF/c kit Ligand (Catalog # BT-SCF) stimulates cell proliferation of the TF-1 human erythroleukemic cell line. The ED50 for this effect is 1.00-8.00 ng/mL.
Equivalent bioactivity of GMP (BT-SCF-GMP), Animal-Free (BT-SCF-AFL) and RUO (Catalog # BT-SCF) grades of Recombinant Human SCF as measured in a cell proliferation assay using TF-1 human erythroleukemic cells (orange, ...read more
2 μg/lane of Recombinant Human SCF/c‑kit Ligand Protein (Catalog # BT-SCF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human SCF Protein, CF Summary

Additional Information
Analyzed by SEC-MALS
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 1.00-8.00 ng/mL.
Source
E. coli-derived human SCF/c-kit Ligand protein
Glu26-Ala189, with a N-terminal Met
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Purity
>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
19 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
18 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
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 Trehalose.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute the 10 μg size at 100 μg/mL in PBS. Reconstitute all other sizes at 500 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 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 alternately spliced isoform of human SCF lacks 28 aa that encompasses 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). SCF is a versatile factor in the differentiation of many specific cell types like spermatogonial stem cells (16) and megakaryocyte progenitors (17). Apart from differentiation, SCF also can maintain stemness in cells. This is the case for human bone marrow mesenchymal cells, which require SCF and hepatocyte growth factor for maintenance (18). Hematopoietic stem cells similarly require SCF from surrounding cells in their niche to maintain their stemness and their progenitors (19). SCF has also improved protocols for continuous generation of cells in culture systems, like granulocytes and macrophages (20).   

For treatment of graft versus host disease, SCF is used in combination with other cytokines to generate myeloid-derived suppressor cells from human umbilical cord blood (21). SCF is also used to generate T cells for cell-based therapies, drug screening and disease modeling (22). In regenerative studies, SCF is applied in wound healing hydrogel as a means of increasing its adhesion strength and tissue regeneration (23).

  1. Ashman, L.K. (1999) Int. J. Biochem. Cell Biol. 31:1037. 
  2. Sette, C. et al. (2000) Int. J. Dev. Biol. 44:599. 
  3. Yoshida, H. et al. (2001) J. Invest. Dermatol. Symp. Proc. 6:1. 
  4. Erlandsson, A. et al. (2004) Exp. Cell Res. 301:201. 
  5. Kapur, R. et al. (2002) Blood 100:1287. 
  6. Wang, C.-H. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:540. 
  7. Bashamboo, A. et al. (2006) J. Cell Sci. 119:3039. 
  8. Reber, L. et al. (2006) Eur. J. Pharmacol. 533:327.
  9. Martin, F.H. et al. (1990) Cell 63:203.
  10. Arakawa, T. et al. (1991) J. Biol. Chem. 266:18942.
  11. Majumdar, M.K. et al. (1994) J. Biol. Chem. 269:1237.
  12. Brannan, C.I. et al. (1991) Proc. Natl. Acad. Sci. 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.
  16. Nasimi, M. et al. (2021) Reprod Sci. 28:963.
  17. Krisch, L. et al. (2021) Int. J. Mol. Sci. 22:8224.
  18. Cao, Z. et al. (2020) Stem Cell Res Ther. 11:1.
  19. Comazzetto, S. et al. (2019) Cell Stem Cell. 24:477.
  20. Bernecker, C. et al. (2019) Stem Cells Dev. 28:1540.
  21. Park, M.Y. et al. (2019) Front Immunol. 10:1.
  22. Netsrithong, R. et al. (2020) Stem Cell Res Ther. 11:1.
  23. Zhang, Li. et al. (2021) Journal Mater Chem B. 29: 5887.

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