Noggin Recombinant Protein | NOG recombinant protein

Human Noggin Protein

Cat. Num. AAA9718671

• Gene Names: NOG; SYM1; SYNS1; SYNS1A
• Purity: >95% as determined by SDS-PAGE.
• Synonyms: Noggin; Human Noggin Protein; Recombinant Human Noggin Protein (Noggin) expressed in Human Cells; SYM1; SYNS1; NOG recombinant protein

• Host: Human Cells
• Purity/Purification: >95% as determined by SDS-PAGE.
• Form/Format: Lyophilized from sterile PBS, pH 7.4.
• Sequence: Amino acid sequence derived from human NOG (NP_005441.1) (Met1-Cys232) was expressed.
• Sequence Length: 232

• Species: Human
• Endotoxin: The Endotoxin level is less than 1.0 EU per mug protein as determined by the LAL method.
• Protein Length: The recombinant human NOG consists of 205 amino acids and predicts a molecular mass of 23.1 kDa.
• Usage Notes: Always centrifuge tubes before opening. It is recommended to reconstitute the lyophilized Human Noggin protein in sterile ddH2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.
• Preparation and Storage: Item should be stored desiccated below -20 degree C. Upon reconstitution, the protein should be stored at 4 degree C between 2-7 days and for future use below -20 degree C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

SDS-Page

(Fig.SDS-PAGE analysis of Human Noggin protein.)

Related Product Information for NOG recombinant protein

Noggin is a secreted protein involved at multiple stages of vertebrate embryonic development including neural induction and is known to exert its effects by inhibiting the bone morphogenetic protein (BMP)-signaling pathway. It binds several BMPs with very high (picomolar) affinities, with a marked preference for BMP2 and BMP4 over BMP7. By binding tightly to BMPs, Noggin prevents BMPs from binding their receptors. Noggin binds the bone morphogenetic proteins (BMP) such as BMP-4 and BMP-7, and inhibits BMP signaling by blocking the molecular interfaces of the binding epitopes for both type I and type II receptors. Interaction of BMP and its antagonist Noggin governs various developmental and cellular processes, including embryonic dorsal-ventral axis, induction of neural tissue, formation of joints in the skeletal system and neurogenesis in the adult brain. Noggin plays a key role in neural induction by inhibiting BMP4, along with other TGF-beta signaling inhibitors such as chordin and follistatin. Mouse knockout experiments have demonstrated that noggin also plays a crucial role in bone development, joint formation, and neural tube fusion.

NCBI and Uniprot Product Information

• NCBI GI #: 4885523
• NCBI GeneID: 9241
• NCBI Accession #: NP_005441.1
• NCBI GenBank Nucleotide #: NP_005441.1
• UniProt Accession #: Q13253
• Molecular Weight: 23.7 kDa
• NCBI Official Full Name: noggin
• NCBI Official Synonym Full Names: noggin
• NCBI Official Symbol: NOG
• NCBI Official Synonym Symbols: SYM1; SYNS1; SYNS1A
• NCBI Protein Information: noggin
• Protein Family: Noggin

NCBI Description

The secreted polypeptide, encoded by this gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta 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 dorsal-ventral 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]