Noggin is a secreted homodimeric glycoprotein that binds to ligands of the TGF-beta family (BMPs) and regulates their activity by inhibiting their access to signaling receptors. Mature human Noggin protein contains an N-terminal acidic region, a central basic heparin-binding segment and a C-terminal cysteine knot structure. Noggin binds different BMPs with variable affinities, antagonizing specific BMPs during skeletal development. Noggin is expressed in defined areas of the adult central nervous system and peripheral tissues such as lung, skeletal muscle and skin. Recombinant Human Noggin expressed in human 293 cells is a glycosylated, disulfide linked homodimer with a molecular weight of 65 kDa.
Alternative Names
NOG
Quantity
10 µg
Regulatory
RUO
Source
HEK293
Host
Human
Endotoxin Level
<1 EU/µg of recombinant protein as determined by the LAL method
Biological Activity Comment
The EC(50) as determined by the dose-dependent inhibition of rh-BMP-4 induced alkaline phosphate production by ATDC5 cells was found to be ≤ 25 ng/mL.
Weight
65 kDa, homodimer, glycosylated
Description
A quick spin of the vial followed by reconstitution in sterile 1xPBS containing 0.1% endotoxin-free recombinant human serum albumin (HSA).
Format
Lyophilized Powder1x PBS
Purity
>95% as determined by SDS-PAGE
Storage
The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months. Avoid repeated freeze/thaw cycles.