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M-CSF的重組小鼠細(xì)胞因子Recombinant Mouse M-CSF

DESCRIPTION

Source E. coliderived

Lys33Glu262,

with an Nterminal

Met

Accession # Q3U4F9

Nterminal

Sequence

Analysis

Met

Structure / Form Disulfidelinked

homodimer

Predicted Molecular

Mass

26 kDa （monomer）

SPECIFICATIONS

SDSPAGE

29 kDa, reducing conditions

Activity Measured in a cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cells. Halenbeck, R. et al. （1989）

Biotechnology 7:710.

The ED50 for this effect is typically 0.5-3 ng/mL.

Endotoxin Level <1.0 EU per 1 μg of the protein by the LAL method.

Purity >97%, by SDSPAGE

under reducing conditions and visualized by silver stain.

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. See Certificate of Analysis for details.

PREPARATION AND STORAGE

Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Shipping The product is shipped at ambient temperature. Upon receipt, store it immediay at the temperature recommended below.

Stability & Storage Use a manual defrost freezer and avoid repeated freezethaw

cycles.

l 12 months from date of receipt, 20

to 70

°C as supplied.

l 1 month, 2 to 8 °C under sterile conditions after reconstitution.

l 3 months, 20

to 70

°C under sterile conditions after reconstitution.

BACKGROUND

MCSF,

also known as CSF1,

is a fourαhelicalbundle

cytokine that is the primary regulator of macrophage survival, proliferation and differentiation （1 3）.

MCSF

is also essential for the survival and proliferation of osteoclast progenitors （1, 4）. MCSF

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）. MCSF

increases during

pregnancy to support implantation and growth of the decidua and placenta （5）. Sources of MCSF

include fibroblasts, activated macrophages, endometrial secretory

epithelium, bone marrow stromal cells and activated endothelial cells （1 5）.

The MCSF

receptor （cfms）

transduces its pleotropic effects and mediates its

endocytosis. MCSF

mRNAs of various sizes occur （3 9）.

Full length mouse MCSF

transcripts encode a 520 amino acid （aa） type I transmembrane （TM） protein with

a 462 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 Nand

Oglycosylated

86 kDa dimer, while the other is modified by both glycosylation and chondroitinsulfate

proteoglycan （PG） to generate a 200 kDa subunit. Although PGmodified

MCSF

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 Nglycosylated

68 kDa TM dimer and a slowly produced 44 kDa secreted dimer （7）.

Although forms may vary in activity and halflife,

all contain the Nterminal

150 aa portion that is necessary and sufficient for interaction with the M CSF

receptor

（10, 11）. The first 229 aa of mature mouse MCSF

shares 87%, 83%, 82% and 81% aa identity with corresponding regions of rat, dog, cow and human MCSF,

respectively （12, 13）. Human MCSF

is active in the mouse, but mouse MCSF

is reported to be speciesspecific.

M-CSF的重組小鼠細(xì)胞因子Recombinant Mouse M-CSF

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, MH.

et al. （2006） J. Immunol. 177:4055.

12. DeLamarter, J.F. et al. （1987） Nucleic Acids Res. 15:2389.

13. Ladner, M.B. et al. （1988） Proc. Natl. Acad. Sci. USA 85:6706.

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