|Calculated MW||92156 Da|
|Purification||Purified IgG prepared by affinity chromatography on Protein A|
|Shelf Life||12 months from date of reconstitution.|
|Other Names||Granulocyte colony-stimulating factor receptor, G-CSF receptor, G-CSF-R, CD114, CSF3R, GCSFR|
|Target/Specificity||Mouse anti-Human CD114 antibody, clone LMM775recognises the human Granulocyte colony-stimulating factor receptor (G-CSF-R) also known as CD114. CD114 is a 836 amino acid, single pass type I transmembrane glycoprotein, a crucial factor in the survival and maturation of cells in the neutrophilic lineage. CD114 contains a single Ig-like C2-type and five fibronectin type-III domains (UniProt: Q99062).Mouse anti-Human CD114 antibody, clone LMM775 binds to an epitope located within the Ig-like domain but does not block binding of G-CSF to its receptor (Leytonet al.2001). Mouse anti-Human CD114 antibody, clone LMM775 does not bind to a mutant G-CSF-R when the Ig-like domain has been substituted with the related gp130 Ig-like domain (Laytonet al.1999). G-CSF stimulates the production of neutrophils and accelerates their maturation in bone marrow (Demetri and Griffin 1991). Expression of CD114 is down regulated on granulocytes but not monocytes following acute exposure to bacterial components including LPS with potential consequences for granulocyte function in the acute response to infection (Dekkerset al.2000). The G-CSF-receptor on monocytes is functional, playing a role in the release of cytokines, either directly or indirectly following bacterial challange (Boneburget al.2000). The G-CSF receptor CD114 has also been implicated in the induction of β-1 integrin mediated adhesion and invasion of pancreatinc cancer cells (Chakrabortyet al.2006).|
|Preservative & Stabilisers||0.09% Sodium azide; Stabilising agent|
|Storage||Storage at +4ºC. DO NOT FREEZE.|
|Precautions||Anti-Human CD114 Antibody, clone LMM775 (RPE) is for research use only and not for use in diagnostic or therapeutic procedures.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
1. Dekkers, P.E. et al. (2000) Granulocyte colony-stimulating factor receptors on granulocytes are down-regulated after endotoxin administration to healthy humans.J Infect Dis. 181: 2067-70. 2. Boneberg, E.M. et al. (2000) Human monocytes express functional receptors for granulocyte colony-stimulating factor that mediate suppression of monokines and interferon-gamma.Blood. 95: 270-6. 3. Layton, J.E. et al. (2001) Identification of ligand-binding site III on the immunoglobulin-like domain of the granulocyte colony-stimulating factor receptor.J Biol Chem. 276: 36779-87. 4. Layton, J.E. et al. (1999) Interaction of granulocyte colony-stimulating factor (G-CSF) with its receptor. Evidence that Glu19 of G-CSF interacts with Arg288 of the receptor.J Biol Chem. 274: 17445-51. 5. Anderson, G. et al. (2006) Thalidomide derivative CC-4047 inhibits osteoclast formation by down-regulation of PU.1.Blood. 107: 3098-105. 6. Chakraborty, A. et al. (2006) Granulocyte Colony-Stimulating Factor Receptor Promotes b1-Integrin–Mediated Adhesion and Invasion of Pancreatic Cancer Cells.In: Conference Abstracts From the 2006 Annual Meeting of the International Society of Gastrointestinal Oncology: Session II: Pancreatic cancer. PGCR 1:1, 2006 (ABSTRACT 208) 7. Layton, J.E. et al. (1997) Neutralising antibodies to the granulocyte colony-stimulating factor receptor recognise both the immunoglobulin-like domain and the cytokine receptor homologous domain.Growth Factors.14: 117-30. 8. Diaz-Romero, J. et al. (2005) Immunophenotypic analysis of human articular chondrocytes: changes in surface markers associated with cell expansion in monolayer culture.J Cell Physiol. 202: 731-42.1. Nicholson, S.E. et al. (1994) Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation. Proc. Natl. Acad. Sci. USA. 91: 2985-2988.
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