ProDots Recombinant Human M-CSF Protein Summary
Additional Information |
Supplied as ready-to-use 5 ug protein balls |
Details of Functionality |
Measured in a cell proliferation assay using M‑NFS‑60 mouse myelogenous leukemia lymphoblast cells. Nakoinz, I. et al. (1990) J. Immunol. 145:860. The ED50 for this effect is 0.5-1.5 ng/mL. |
Source |
E. coli-derived human M-CSF protein Glu33 - Ser190, with an N-terminal Met |
Accession # |
|
N-terminal Sequence |
Met |
Protein/Peptide Type |
ProDots Proteins |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
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. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. • 6 months from date of receipt at room temperature. • 12 months from date of receipt at 2-8 °C as supplied. • 1 month at 2-8 °C under sterile conditions after reconstitution. • 3 months at -20 to -80 °C under sterile conditions after reconstitution. |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
For a stock solution, reconstitute at 50-500 μg/mL in sterile PBS, or simply roll ProDot® directly into cell culture medium.
|
Notes
726881.0
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for ProDots Recombinant Human M-CSF Protein
Background
M-CSF, also known as CSF-1, is a four-alpha-helical-bundle cytokine that is the primary regulator of macrophage survival, proliferation and differentiation. M-CSF is also essential for the survival and proliferation of osteoclast progenitors. M-CSF also primes and enhances macrophage killing of tumor cells and microorganisms, regulates the release of cytokines and other inflammatory modulators from macrophages, and stimulates pinocytosis. M-CSF increases during pregnancy to support implantation and growth of the decidua and placenta. Sources of M-CSF include fibroblasts, activated macrophages, endometrial secretory epithelium, bone marrow stromal cells and activated endothelial cells. The M-CSF receptor (c-fms) transduces its pleotropic effects and mediates its endocytosis. M-CSF mRNAs of various sizes occur. Full length human M-CSF transcripts encode a 522 amino acid (aa) type I transmembrane (TM) protein with a 464 aa extracellular region, a 21 aa TM domain, and a 37 aa cytoplasmic tail that forms a 140 kDa covalent dimer. Differential processing produces two proteolytically cleaved, secreted dimers. One is an N- and O- glycosylated 86 kDa dimer, while the other is modified by both glycosylation and chondroitin-sulfate proteoglycan (PG) to generate a 200 kDa subunit. Although PG-modified M-CSF can circulate, it may be immobilized by attachment to type V collagen. Shorter transcripts encode M-CSF that lack cleavage and PG sites and produce an N-glycosylated 68 kDa TM dimer and a slowly produced 44 kDa secreted dimer. Although forms may vary in activity and half-life, all contain the N-terminal 150 aa portion that is necessary and sufficient for interaction with the M-CSF receptor. The first 223 aa of mature human M-CSF shares 88%, 86%, 81% and 74% aa identity with corresponding regions of dog, cow, mouse and rat M-CSF, respectively. Human M-CSF is active in the mouse, but mouse M-CSF is reported to be species-specific.
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