Recombinant Human Kit ligand (KITLG) is produced in a mammalian expression system and comes with a C-terminal 6xHis-tag for easier purification and detection. This partial protein covers amino acids 26-214 and appears to maintain high purity levels of over 95% based on SDS-PAGE analysis. The protein shows biological activity with an ED50 of 2-10 ng/ml in TF-1 cell proliferation assays. Endotoxin levels stay below 1.0 EU/µg, which likely minimizes interference in experimental work.
KITLG, commonly called stem cell factor, seems to play a central role in hematopoiesis by acting as a ligand for the c-Kit receptor. The protein is involved in key signaling pathways that may influence cell survival, proliferation, and differentiation—particularly in hematopoietic cells. Given these regulatory functions, KITLG has become an important target in stem cell biology and oncology research, potentially offering insights into how cells grow and develop.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Cell Proliferation and Viability Assays
This recombinant KITLG protein can stimulate cell proliferation in hematopoietic cell lines and primary cells that express the KIT receptor. The established ED50 of 2-10 ng/ml in TF-1 cells gives researchers a validated concentration range for dose-response studies. Scientists might use this protein to examine cell cycle progression, survival signaling pathways, and growth factor dependencies across different blood cell lineages. High purity and low endotoxin levels make it appropriate for sensitive cell culture work where contamination could skew results.
2. KIT Receptor Binding and Signaling Studies
Biologically active KITLG can work as a ligand in receptor-binding assays to characterize KIT receptor expression and affinity on various cell types. Research teams may study downstream signaling cascades that activate when KIT and KITLG interact, including phosphorylation events and pathway activation. The C-terminal His-tag allows for detection and quantification in binding studies through anti-His antibodies or His-specific detection reagents. Such studies could reveal important details about receptor pharmacology and signal transduction mechanisms.
3. Hematopoietic Stem Cell Research
KITLG protein may prove valuable in ex vivo culture systems designed to maintain and expand hematopoietic stem and progenitor cells for research. Its ability to promote cell proliferation makes it potentially useful for studying stem cell self-renewal, differentiation, and lineage commitment processes. Scientists can examine how KITLG signaling influences hematopoietic development and homeostasis using primary bone marrow or cord blood samples. The mammalian expression system likely ensures proper protein folding and post-translational modifications that are relevant to human biology.
4. Antibody Development and Validation
The recombinant KITLG protein works as an antigen for developing and characterizing anti-KITLG antibodies in research applications. Its His-tag makes protein purification and immobilization more straightforward for immunization protocols and antibody screening assays. Research groups can apply this protein in ELISA, Western blot, and other immunoassays to validate antibody specificity and determine binding characteristics. High purity should minimize cross-reactivity with contaminating proteins during antibody development.
5. Protein-Protein Interaction Studies
KITLG protein may be helpful in pull-down assays and co-immunoprecipitation experiments to identify and characterize protein interactions involving the KIT ligand. The C-terminal His-tag enables immobilization on metal affinity resins for capturing interacting proteins from cell lysates or purified protein mixtures. Researchers might investigate potential co-receptors, signaling adapters, or regulatory proteins that associate with KITLG. These studies could uncover novel molecular mechanisms and regulatory networks within KITLG signaling pathways.
