N6784
Noggin/Fc Chimera from mouse
>95% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
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About This Item
Recommended Products
biological source
mouse
Quality Level
recombinant
expressed in NSO cells
assay
>95% (SDS-PAGE)
form
lyophilized powder
mol wt
55-60 kDa by SDS-PAGE (reducing)
calculated mol wt 50 kDa
packaging
pkg of 50 μg
impurities
endotoxin, tested
UniProt accession no.
storage temp.
−20°C
Gene Information
mouse ... Nog(18121)
Biochem/physiol Actions
Binds and blocks the acitivity of bone morphogenetic proteins (BMPs). Mature mouse noggin shares 99% and 83% sequence identity with human and Xenopus noggin, respectively.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.
Analysis Note
The biological activity is measured by its ability to inhibit recombinant human BMP-4 induced alkaline phosphatase activity in ATDC5 cells.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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D A Lim et al.
Neuron, 28(3), 713-726 (2001-02-13)
Large numbers of new neurons are born continuously in the adult subventricular zone (SVZ). The molecular niche of SVZ stem cells is poorly understood. Here, we show that the bone morphogenetic protein (BMP) antagonist Noggin is expressed by ependymal cells
Impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis in noggin-overexpressing mice.
Wu XB
The Journal of Clinical Investigation (2003)
The expression patterns of gremlin 1 and noggin in normal adult and tumor tissues.
Laurila R
International Journal of Clinical and Experimental Pathology (2013)
A H Reddi
Arthritis research, 3(1), 1-5 (2001-02-15)
This commentary is a concise discussion of the interactions between bone morphogenetic proteins (BMPs) and their binding proteins in bone and cartilage morphogenesis. BMPs are a family of growth and differentiation factors, and they act on mesenchymal cells to induce
Human disease-causing NOG missense mutations: effects on noggin secretion, dimer formation, and bone morphogenetic protein binding.
Marcelino J
Proceedings of the National Academy of Sciences of the USA (2001)
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