Human Noggin Protein (E. coli), Research Grade, Unconjugated
Artikelnummer:
ABS-NON-H5118-20UG
Hersteller Artikelnummer:
NON-H5118-20ug
Alternativnummer:
ABS-NON-H5118-20UG
Hersteller:
AcroBiosystems
Wirt:
E. coli
Kategorie:
Proteine/Peptide
Spezies Reaktivität:
Human
Konjugation:
Unconjugated
The secreted polypeptide, encoded by this gene, binds and inactivates members of the transforming growth factorbeta (TGFbeta) superfamily signaling proteins, such as bone morphogenetic protein4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGFbeta superfamily, this protein may have a principal role in creating morphogenic gradients. The protein appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsalventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of the ortholog suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified, both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as this gene. All of these mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of this human gene is highly homologous to that of Xenopus, rat and mouse. [provided by RefSeq, Jul 2008] - Proteine/Peptide
Human Noggin Protein (E. coli), Research Grade on SDS-PAGE under reducing (R) and under non-reducing (NR) conditions. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
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