GM-CSF Antibody

Recombinant Human GM‑CSF (Catalog # 215-GM) stimulates proliferation in the TF‑1 human erythroleukemic cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human GM‑CSF (0.5 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human GM‑CSF Antigen Affinity-purified Polyclonal Antibody (Catalog # AF‑215‑NA). The ND50 is typically 0.08-0.16 µg/mL.

• Reactivity: Hu
• Applications: WB, B/N
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Unconjugated
• Concentration: LYOPH

GM-CSF Antibody Summary

• Immunogen: E. coli-derived recombinant human GM-CSF
  Ala18-Glu144
  Accession # P04141
• Specificity: Detects human GM‑CSF in direct ELISAs and Western blots. In direct ELISAs, less than 1% cross‑reactivity with recombinant mouse GM‑CSF is observed. Neutralizes the biological activity of both recombinant human GM‑CSF and natural human GM‑CSF.
• Source: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Gene: CSF2
• Purity Statement: Antigen Affinity-purified
• Endotoxin Note: <0.10 EU per 1 μg of the antibody by the LAL method.

Applications/Dilutions

• Dilutions:
  • Neutralization 0.08-0.16 ug/mL
  • Western Blot 0.1 ug/mL

Packaging, Storage & Formulations

• 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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
• Preservative: No Preservative
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute at 0.2 mg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for GM-CSF Antibody

• colony stimulating factor 2 (granulocyte-macrophage)
• Colony-stimulating factor
• CSF
• CSF2
• CSF-2
• GMCSF
• GM-CSF
• GMCSFgranulocyte-macrophage colony-stimulating factor
• granulocyte-macrophage colony stimulating factor
• MGC131935
• MGC138897
• Molgramostim
• molgramostin
• Sargramostim

Background

GM-CSF was initially characterized as a factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It is also a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. GM-CSF is produced by a number of different cell types (including T cells, B cells, macrophages, mast cells, endothelial cells, fibroblasts, and adipocytes) in response to cytokine or inflammatory stimuli. On mature hematopoietic cells, GM-CSF is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages, and eosinophils (1, 2). GM-CSF promotes a Th1 biased immune response, angiogenesis, allergic inflammation, and the development of autoimmunity (3‑5). It shows clinical effectiveness in ameliorating chemotherapy-induced neutropenia, and GM-CSF transfected tumor cells are utilized as cancer vaccines (6, 7). The 22 kDa glycosylated GM-CSF, similar to IL-3 and IL-5, is a cytokine with a core of four bundled alpha ‑helices (8‑12). Mature human GM-CSF shares 63%‑70% amino acid sequence identity with canine, feline, porcine, and rat GM-CSF and 54% with mouse GM-CSF. GM-CSF exerts its biological effects through a heterodimeric receptor complex composed of GM-CSF R alpha /CD116 and the signal transducing common beta  chain (CD131) which is also a component of the high-affinity receptors for IL-3 and IL-5 (13, 14). In addition, GM-CSF binds a naturally occurring soluble form of GM-CSF R alpha (15). Human GM-CSF is active on canine and feline cells but not on murine cells (16‑18).

1. Martinez-Moczygemba, M. and D.P. Huston (2003) J. Allergy Clin. Immunol. 112:653.
2. Barreda, D.R. et al. (2004) Dev. Comp. Immunol. 28:509.
3. Eksioglu, E.A. et al. (2007) Exp. Hematol. 35:1163.
4. Cao, Y. (2007) J. Clin. Invest. 117:2362.
5. Fleetwood, A.J. et al. (2005) Crit. Rev. Immunol. 25:405.
6. Heuser, M. et al. (2007) Semin. Hematol. 44:148.
7. Hege, K.M. et al. (2006) Int. Rev. Immunol. 25:321.
8. Kaushansky, K. et al. (1992) Biochemistry 31:1881.
9. Diederichs, K. et al. (1991) Science 254:1779. 
10. Cantrell, M.A. et al. (1985) Proc. Natl. Acad. Sci. 82:6250.
11. Lee, F. et al. (1985) Proc. Natl. Acad. Sci. 82:4360.
12. Wong, G.G. et al. (1985) Science 228:810.
13. Onetto-Pothier, N. et al. (1990) Blood 75:59.
14. Hayashida, K. et al. (1990) Proc. Natl. Acad. Sci. 87:9655.
15. Pelley, J.L. et al. (2007) Exp. Hematol. 35:1483.
16. Hogge, G.S. et al. (1990) Cancer Gene Ther. 6:26.
17. Sprague, W.S. et al. (2005) J. Comp. Pathol. 133:136.
18. Shanafelt, A.B. et al. (1991) J. Biol. Chem. 266:13804.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for GM-CSF Antibody (AF-215-NA)(10)

Publications using AF-215-NA

• AV Smirnov, GV Kontsevaya, TA Shnaider, AM Yunusova, NA Feofanova, LA Gerlinskay, IA Serova, OL Serov, NR Battulin Evaluation of the alpha-casein (CSN1S1) locus as a potential target for a site-specific transgene integration Scientific Reports, 2022-05-14;12(1):7983. 2022-05-14 [PMID: 35568783] (IHC, Western Blot, Mouse)
• J Li, A Wuethrich, AAI Sina, HH Cheng, Y Wang, A Behren, PN Mainwaring, M Trau A digital single-molecule nanopillar SERS platform for predicting and monitoring immune toxicities in immunotherapy Nature Communications, 2021-02-17;12(1):1087. 2021-02-17 [PMID: 33597530] (ELISA Capture, Human)
• Shuvasree SenGupta, Madhavi J Rane, Silvia M Uriarte, Cassandra Woolley, Thomas C Mitchell Human neutrophils depend on extrinsic factors produced by monocytes for their survival response to TLR4 stimulation Innate Immunity 11/1/2019 [PMID: 31480890]
• Kumar D, Moore R, Nash A, Springel E, Mercer B, Philipson E, Mansour J, Moore J Decidual GM-CSF is a critical common intermediate necessary for thrombin and TNF induced in-vitro fetal membrane weakening. Placenta, 2014-10-12;35(12):1049-56. 2014-10-12 [PMID: 25454284] (Neutralization, Human)
• Hashimoto A, Tanaka T, Itoh Y, Yamagata A, Kitamura N, Tazawa R, Nakagaki K, Nakata K Low concentrations of recombinant granulocyte macrophage-colony stimulating factor derived from Chinese hamster ovary cells augments long-term bioactivity with delayed clearance in vitro. Cytokine, 2014-05-09;68(2):118-26. 2014-05-09 [PMID: 24813650] (Neutralization, Human)
• Claudia M. Gutschalk, Archana K. Yanamandra, Nina Linde, Alice Meides, Sofia Depner, Margareta M. Mueller GM-CSF enhances tumor invasion by elevated MMP-2, -9, and -26 expression Cancer Medicine 4/1/2013 [PMID: 23634280]
• Daryadel A, Grifone RF, Simon HU, Yousefi S Apoptotic neutrophils release macrophage migration inhibitory factor upon stimulation with tumor necrosis factor-alpha. J. Biol. Chem., 2006-07-21;281(37):27653-61. 2006-07-21 [PMID: 16861224] (ICC, Human)
• Bartemes KR, Cooper KM, Drain KL, Kita H Secretory IgA induces antigen-independent eosinophil survival and cytokine production without inducing effector functions. J. Allergy Clin. Immunol., 2005-10-01;116(4):827-35. 2005-10-01 [PMID: 16210057] (Neutralization, Human)
• Channon JY, Miselis KA, Minns LA, Dutta C, Kasper LH Toxoplasma gondii induces granulocyte colony-stimulating factor and granulocyte-macrophage colony-stimulating factor secretion by human fibroblasts: implications for neutrophil apoptosis. Infect. Immun., 2002-11-01;70(11):6048-57. 2002-11-01 [PMID: 12379681] (Neutralization, Human)
• Sato E, Koyama S Bleomycin stimulates lung fibroblast and epithelial cell lines to release eosinophil chemotactic activity. Eur. Respir. J., 2000-11-01;16(5):951-8. 2000-11-01 [PMID: 11153598] (Neutralization, Human)

Bioinformatics

• Gene Symbol: CSF2
• Uniprot:
  • P04141(Human)