Human SCF
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| Cat-Nr. | 100-097S |
| Size | 2 µg |
| Price | 65 € |
| Source | E. coli |
| Formulation | lyophilized |
| Purity Confirmation | > 98% by SDS-PAGE |
| Length [aa] | 165 |
| Molecular Weight | 18.5 kDa |
| N Terminal Sequence | MEGIC |
| Endotoxin Levels | < 0.1 ng per µg of human SCF |
| Biological Activity | The ED50 as determined by the dose-dependent stimulation of human TF-1 cells is in the range of 1 - 5 ng/ml. The WHO standard #91/682 was used as a control. |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | Centrifuge vial prior to opening. Human SCF should be reconstituted in water to a concentration of 0.1 mg/ml. This solution can be further diluted in water or other buffer solutions or stored at -20°C. |
| Stability and Storage | Lyophilized SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). |
| Synonyms | KITLG; SF; MGF; SCF; FPH2; KL-1; Kitl; SHEP7; kit-ligand; stem cell factor; Mast cell growth factor; c-Kit ligand |
| Description | 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. It promotes the survival, differentiation, and mobilization of multiple cell types including myeloid, erythroid, megakaryocytic, lymphoid, germ cell, and melanocyte progenitors. SCF is a primary growth and activation factor for mast cells and eosinophils. Mature mouse SCF consists of a 189 amino acids (aa) extracellular domain (ECD), a 23 aa transmembrane segment, and a 36 aa cytoplasmic tail. The ECD shows both N-linked and O-linked glycosylation. 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. An alternatively spliced isoform of mouse SCF lacks 28 aa that encompasses the primary proteolytic recognition site. Within the ECD of the short isoform (corresponding to this recombinant protein), mouse SCF shares 93% aa sequence identity with rat SCF and 72% to 75% with canine, feline, and human SCF. Rat SCF is active on mouse and human cells, but human SCF is only weakly active on mouse cells. Non-covalent dimers of transmembrane or soluble SCF interact with the receptor tyrosine kinase SCF R/c-kit to trigger receptor dimerization and signaling. SCF assists in the recovery of cardiac function following myocardial infarction by increasing the number of cardiomyocytes and vascular channels. |
| Protein Sequence | MEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVA |
| Uniprot ID | P21583 |
| Protein RefSeq | NP_000890 |
| mRNA RefSeq | NM_000899 |
Figures
SDS-PAGE analysis of recombinant human SCF. Sample was loaded in 15% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.
Dose-dependent stimulation of proliferation in TF-1 cells by recombinant human SCF and the WHO standard #91/682. Values are the means (±SD) of triplicate determinations and expressed as percentage of control.
Reference
- Antileukemic potential of methylated indolequinone MAC681 through immunogenic necroptosis and PARP1 degradation. B. Orlikova-Boyer et al., Biomark Res. 2024; 12: 47.
- Sphingolipid-mediated inflammatory signaling leading to autophagy inhibition converts erythropoiesis to myelopoiesis in human hematopoietic stem/progenitor cells. M. Orsini et al., Cell Death Differ. 2019 Sep; 26(9): 1796–1812.
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