M-CSF Protein, Human, Recombinant (His Tag)

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M-CSF Protein, Human, Recombinant (His Tag): Product Information

Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Measured by its binding ability in a functional ELISA.
2. Immobilized human CSF1R (Cat:10161-H08H) at 10 μg/mL (100 μl/well) can bind biotinylated human CSF-1 (Cat:11792-H08H).
The EC50 of biotinylated human CSF-1 (Cat:11792-H08H) is 8 ng/mL.
3. Measured in a cell proliferation assay using M‑NFS‑60 mouse myelogenous leukemia lymphoblast cells.
The ED50 for this effect is typically 2-8 ng/mL.
Protein Construction
A DNA sequence encoding the N-terminal fragment (Met 1-Asn 190) of human CSF1 (P09603-1) was fused with a polyhistidine tag at the C-terminus.Human and Cynomolgus CSF1 sequences are identical.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Glu 22
Molecule Mass
The recombinant human CSF1 consists of 169 amino acids and predictes a molecular mass of 19.8 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhCSF1 is approximately 27-32 kDa band due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

M-CSF Protein, Human, Recombinant (His Tag): Images

Measured in a cell proliferation assay using M‑NFS‑60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is typically 2-8 ng/mL.

M-CSF Protein, Human, Recombinant (His Tag): Alternative Names

CSF-1 Protein, Human; M-CSF Protein, Human; MCSF Protein, Human

M-CSF Background Information

Macrophage colony-stimulating factor 1, also known as CSF-1, M-CSF, Lanimostim and CSF1, is a single-pass membrane protein which is disulfide-linked as a homodimer or heterodimer. Granulocyte / macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. M-CSF/CSF-1 is known to facilitate monocyte survival, monocyte-to-macrophage conversion, and macrophage proliferation. M-CSF/CSF-1 is a secreted cytokine which influences hemopoietic stem cells to differentiate into macrophages or other related cell types. It binds to the Colony stimulating factor 1 receptor. M-CSF/CSF-1 may also be involved in development of the placenta. The active form of M-CSF/CSF-1 is found extracellularly as a disulfide-linked homodimer, and is thought to be produced by proteolytic cleavage of membrane-bound precursors. M-CSF/CSF-1 induces cells of the monocyte/macrophage lineage. It also plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy. Upregulation of M-CSF/CSF-1 in the infarcted myocardium may have an active role in healing not only through its effects on cells of monocyte/macrophage lineage, but also by regulating endothelial cell chemokine expression.
Full Name
colony stimulating factor 1 (macrophage)
References
    1. Pandit J. et al., 1992, Science. 258: 1358-62.
    2. Tokai M. et al., 2000, J Bacteriol. 182 (10): 2865-8.
    3. Fan X. et al., 2001, Am J Physiol Endocrinol Metab. 280 (1): E103-11.
    4. Frangogiannis NG. et al., 2003, Am J Physiol Heart Circ Physiol. 285 (2): H483-92.
    5. Cupp JS. et al., 2007, Am J Surg Pathol. 31 (6): 970-6.
  • A potent in vivo anti-tumor efficacy of novel recombinant type I interferon
    Author
    Zhang, K;Yin, XF;Yang, YQ;Li, HL;Xu, YN;Chen, LY;Liu, XJ;Yuan, SJ;Fang, XL;Xiao, J;Wu, S;Xu, H;Chu, L;Katlinski, KV;Katlinskaya, YV;Guo, RB;Wei, GW;Wang, DC;Liu, X;Fuchs, SY;
    Year
    2016
    Journal
    Clin. Cancer Res.
    Application
    binding
  • A potent in vivo anti-tumor efficacy of novel recombinant type I interferon
    Author
    Zhang, K;Yin, XF;Yang, YQ;Li, HL;Xu, YN;Chen, LY;Liu, XJ;Yuan, SJ;Fang, XL;Xiao, J;Wu, S;Xu, H;Chu, L;Katlinski, KV;Katlinskaya, YV;Guo, RB;Wei, GW;Wang, DC;Liu, X;Fuchs, SY;
    Year
    2016
    Journal
    Clin. Cancer Res.
    Application
    binding
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