Noggin Human, HEK
HEK293 Cells.
Description
Noggin produced in HEK293 cells is a polypeptide chain containing 211 amino acids (28-232a.a.) and having a molecular mass of 23.8kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
Noggin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
This product consists of recombinant human Noggin, produced in HEK293 cells. It is a polypeptide chain with 211 amino acids (28-232a.a.) and a molecular mass of 23.8kDa. When analyzed using SDS-PAGE, the molecular size appears between 28-40kDa. The Noggin protein features a 6 amino acid His tag at the C-Terminus and is purified through proprietary chromatographic techniques.
| This recombinant human Noggin protein, derived from HEK293 cells, is supplied in a solution format. The concentration is 0.25mg/ml, and the solution contains 50mM MES (pH 6.5) and 30% glycerol. |
HEK293 Cells.
Product Science Overview
Recombinant human Noggin is expressed in human embryonic kidney (HEK) 293 cells. This expression system is advantageous because it allows for human-like glycosylation and folding of the protein, which often supports better stability and functionality in cell culture. The recombinant protein is typically produced as a glycoprotein with a calculated molecular mass of 23 kDa, although it migrates as a 25 kDa band on SDS-PAGE due to glycosylation .
Noggin is a 232 amino acid-secreted glycosylated protein that forms covalently linked homodimers. It has a high affinity for BMP4 and other BMPs, effectively inhibiting their activity. The protein possesses a cystine-knot domain, which includes two β-strand finger-like loops, essential for its binding to BMPs .
Noggin is essential for normal development in mice and humans. It is required for cartilage morphogenesis and joint formation. In developing embryos, Noggin is produced in the mesoderm and plays a critical role in the formation of gradients of BMP activity. Knockout mice lacking Noggin expression die at birth due to multiple defects, including bony fusion of the appendicular skeleton .
In addition to its role in development, Noggin has been shown to promote the growth of human embryonic stem cells (hESCs) in culture. When incorporated into the extracellular matrix or used as a medium supplement, Noggin helps maintain stem cells in a pluripotent state and prevents spontaneous differentiation .
Recombinant human Noggin is widely used in cell culture and developmental biology research. It is used as a supplement in media for the isolation and culture of various cell types, including human enteroids and pancreatic endoderm cells. Noggin is also used in studies investigating the inhibition of BMP signaling and its effects on cell growth and differentiation .
