Colony Stimulating Factor 2 (Granulocyte-Macrophage) (CSF2) (AA 18-144), (Mature) (Active) protein (His tag)

Details zu Produkt Nr. ABIN2001912, Anbieter: Anmelden zum Anzeigen
Proteinname
  • CSF2
  • GM-CSF
  • GMCSF
  • CSF
  • Csfgm
  • Gm-CSf
  • MGI-IGM
  • Gm-csf
  • Gmcsf
  • granulocyte-macrophage colony-stimulating-factor
  • colony stimulating factor 2 (granulocyte-macrophage)
  • granulocyte-macrophage colony-stimulating factor
  • granulocyte-macrophage colony stimulating factor
  • GM-CSF
  • CSF2
  • Csf2
Proteineigenschaft
AA 18-144, Mature
29
6
6
4
4
4
4
2
1
1
1
1
1
1
1
Spezies
Human
77
24
14
6
5
4
2
1
1
1
1
1
1
Quelle
Human Cells
66
9
7
7
4
3
3
2
2
2
2
1
1
1
1
1
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Aufreinigungstag / Konjugat
Dieses CSF2 Protein ist gelabelt mit His tag.
Applikation
Functional Studies (Func), SDS-PAGE (SDS)
Optionen
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Produktmerkmale The recombinant human GM-CSF consists of 147 amino acids and has a predicted molecular mass of 16.9 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh GM-CSF is approximately 24-27 kDa due to glycosylation.

Protein Structure: A DNA sequence encoding the mature form of human GM-CSF (NP_000749.2) (Ala 18-Glu 144) was expressed, with a polyhistidine tag at the N-terminus.
Predicted N-Term: His
Reinheit > 92 % as determined by SDS-PAGE
Endotoxin-Niveau < 1.0 EU per μg of the protein as determined by the LAL method
ProductDetails: Biological Activity Comment Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is typically 0.1-0.6 ng/mL.
Hintergrund Synonyms: GM-CSF,GMCSF
Molekulargewicht 16.9 kDa, 24-27 kDa
NCBI Accession NP_000749
Pathways JAK-STAT Signalweg, Cellular Response to Molecule of Bacterial Origin
Applikationshinweise Optimal working dilution should be determined by the investigator.
Beschränkungen Nur für Forschungszwecke einsetzbar
Format Lyophilized
Buffer Lyophilized from sterile PBS, pH 7.4
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.
Handhabung Avoid repeated freeze-thaw cycles. It is recommended that the protein be aliquoted for optimal storage.
Lagerung -20 °C,-80 °C
Informationen zur Lagerung Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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.
Haltbarkeit 12 months
Bilder des Herstellers
SDS-PAGE (SDS) image for Colony Stimulating Factor 2 (Granulocyte-Macrophage) (CSF2) (AA 18-144), (Mature) (Active) protein (His tag) (ABIN2001912) Colony Stimulating Factor 2 (Granulocyte-Macrophage) (CSF2) (AA 18-144), (Mature) (Active) protein (His tag)
Allgemeine Veröffentlichungen Volmar, Ait-Ghezala, Frieling, Paris, Mullan: "The granulocyte macrophage colony stimulating factor (GM-CSF) regulates amyloid beta (Abeta) production." in: Cytokine, Vol. 42, Issue 3, pp. 336-44, 2008 (PubMed).

Kato, Noma, Kitagawa, Takahashi, Oshitani, Kitagawa: "Distinct role of c-Jun N-terminal kinase isoforms in human neutrophil apoptosis regulated by tumor necrosis factor-alpha and granulocyte-macrophage colony-stimulating factor." in: Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research, Vol. 28, Issue 4, pp. 235-43, 2008 (PubMed).

Ebner, Bandion, Binder, de Martin, Schmid: "GMCSF activates NF-kappaB via direct interaction of the GMCSF receptor with IkappaB kinase beta." in: Blood, Vol. 102, Issue 1, pp. 192-9, 2003 (PubMed).

Hamilton: "GM-CSF in inflammation and autoimmunity." in: Trends in immunology, Vol. 23, Issue 8, pp. 403-8, 2002 (PubMed).

Frolova, Dolganov, Mazo, Smirnov, Copeland, Stewart, OBrien, Dean: "Linkage mapping of the human CSF2 and IL3 genes." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 11, pp. 4821-4, 1991 (PubMed).