Recombinant Human M-CSF Biotinylated Protein, CF

R&D Systems, part of Bio-Techne | Catalog # BT216

Biotinylated
R&D Systems, part of Bio-Techne
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BT216-025
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Key Product Details

Source

E. coli

Accession #

NP_757350.2

Structure / Form

Disulfide-linked homodimer
Biotinylated via amines

Conjugate

Biotin

Applications

Bioactivity

View all M-CSF Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human M-CSF protein
Glu33-Ser190, with an N-terminal Met

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

18.5 kDa

SDS-PAGE

15-22 kDa, under reducing conditions.

Activity

Measured by its binding ability in a functional ELISA.
When Recombinant Human M-CSF R/CD115 Fc Chimera Protein  (Catalog # 329-MR) is immobilized at 0.5 μg/mL (100 µL/well), the concentration of &Biotinylated Recombinant Human M‑CSF (Catalog # BT216) that produces 50% of the optimal binding response is 1.50-15.0 ng/mL.

Scientific Data Images for Recombinant Human M-CSF Biotinylated Protein, CF

Biotinylated Recombinant Human M‑CSF Protein Binding Activity.

When Recombinant Human M-CSF R/CD115 Fc Chimera Protein (329-MR) is immobilized at 0.5 μg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human M‑CSF Protein (Catalog # BT216) that produces 50% of the optimal binding response is 1.50-15.0 ng/mL.

Biotinylated Recombinant Human M‑CSF Protein SDS-PAGE.

2 μg/lane of Biotinylated Recombinant Human M‑CSF Protein (Catalog # BT216) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 15-22 kDa and 30-40 kDa, respectively.

Formulation, Preparation and Storage

BT216
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 250 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: M-CSF

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 (1-3). M-CSF is also essential for the survival and proliferation of osteoclast progenitors (1, 4). 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 (2, 3). M-CSF increases during pregnancy to support implantation and growth of the decidua and placenta (5). Sources of M-CSF include fibroblasts, activated macrophages, endometrial secretory epithelium, bone marrow stromal cells and activated endothelial cells (1-5). The M-CSF receptor (c-fms) transduces its pleotropic effects and mediates its endocytosis. M-CSF mRNAs of various sizes occur (3-9). 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 (8). Shorter transcripts encode
M‑CSF that lacks cleavage and PG sites and produces an N-glycosylated 68 kDa TM dimer and a slowly produced 44 kDa secreted dimer (7). 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 (10, 11). 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 (12, 13). Human M-CSF is active in the mouse, but mouse M-CSF is reported to be species-specific.

References

  1. Pixley, F.J. and E.R. Stanley (2004) Trends Cell Biol. 14:628.
  2. Chitu, V. and E.R. Stanley (2006) Curr. Opin. Immunol. 18:39.
  3. Fixe, P. and V. Praloran (1997) Eur. Cytokine Netw. 8:125.
  4. Ryan, G.R. et al. (2001) Blood 98:74.
  5. Makrigiannakis, A. et al. (2006) Trends Endocrinol. Metab. 17:178.
  6. Nandi, S. et al. (2006) Blood 107:786.
  7. Rettenmier, C.W. and M.F. Roussel (1988) Mol. Cell Biol. 8:5026.
  8. Suzu, S. et al. (1992) J. Biol. Chem. 267:16812.
  9. Manos, M.M. (1988) Mol. Cell. Biol. 8:5035.
  10. Koths, K. (1997) Mol. Reprod. Dev. 46:31.
  11. Jang, M-H. et al. (2006) J. Immunol. 177:4055.
  12. Kawasaki, E.S. et al. (1985) Science 230: 291.
  13. Wong, G.G. et al. (1987) Science 235:1504.

Long Name

Macrophage Colony Stimulating Factor

Alternate Names

CSF-1, CSF1, Lanimostim, MCSF

Entrez Gene IDs

1435 (Human); 12977 (Mouse)

Gene Symbol

CSF1

UniProt

NP_757350.2

Additional M-CSF Products

Product Documents for Recombinant Human M-CSF Biotinylated Protein, CF

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