Noggin / NOG Recombinant Protein | NOG recombinant protein

Recombinant Human Noggin / NOG Protein (Fc tag)

Cat. Num. AAA2546373

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

• Host: Human Cells
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5
• Sequence Length: 232

• Application Notes: The recombinant human Noggin/Fc is a disulfide-linked homodimeric protein after removal of the signal peptide. Each monomer comprises 443 amino acids and has a predicted molecular mass of 49.8 kDa. As a result of glycosylation, the apparent molecular mass of rhNoggin/Fc monomer is approximately 58-62 kDa in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Gln 28
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for NOG recombinant protein

Background: 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.

Description: A DNA sequence encoding the human Noggin precursor (NP_005441.1) (Met 1-Cys 232) was fused with the Fc region of human IgG1 at the C-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 4885523
• NCBI GeneID: 9241
• NCBI Accession #: NP_005441.1
• NCBI GenBank Nucleotide #: NM_005450.4
• UniProt Accession #: Q13253
• Molecular Weight: 25,774 Da
• 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
• UniProt Protein Name: Noggin
• Protein Family: Noggin
• UniProt Gene Name: NOG

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]

Uniprot Description

NOG: Essential for cartilage morphogenesis and joint formation. Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Defects in NOG are a cause of symphalangism proximal syndrome (SYM1). SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone. Defects in NOG are the cause of multiple synostoses syndrome type 1 (SYNS1); also known as synostoses, multiple, with brachydactyly/symphalangism-brachydactyly syndrome. SYNS1 is characterized by tubular-shaped (hemicylindrical) nose with lack of alar flare, otosclerotic deafness, and multiple progressive joint fusions commencing in the hand. The joint fusions are progressive, commencing in the fifth proximal interphalangeal joint in early childhood (or at birth in some individuals) and progressing in an ulnar-to-radial and proximal- to-distal direction. With increasing age, ankylosis of other joints, including the cervical vertebrae, hips, and humeroradial joints, develop. Defects in NOG are the cause of tarsal-carpal coalition syndrome (TCC). TCC is an autosomal dominant disorder characterized by fusion of the carpals, tarsals and phalanges, short first metacarpals causing brachydactyly, and humeroradial fusion. TCC is allelic to SYM1, and different mutations in NOG can result in either TCC or SYM1 in different families. Defects in NOG are a cause of stapes ankylosis with broad thumb and toes (SABTS); also known as Teunissen- Cremers syndrome. SABTS is a congenital autosomal dominant disorder that includes hyperopia, a hemicylindrical nose, broad thumbs, great toes, and other minor skeletal anomalies but lacked carpal and tarsal fusion and symphalangism. Defects in NOG are the cause of brachydactyly type B2 (BDB2). BDB2 is a subtype of brachydactyly characterized by hypoplasia/aplasia of distal phalanges in combination with distal symphalangism, fusion of carpal/tarsal bones, and partial cutaneous syndactyly. Belongs to the noggin family.

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 17q22

Cellular Component: extracellular region; extracellular space

Molecular Function: cytokine binding; protein binding; protein homodimerization activity

Biological Process: atrial cardiac muscle morphogenesis; BMP signaling pathway; cell differentiation in hindbrain; dorsal/ventral pattern formation; embryonic digit morphogenesis; embryonic skeletal development; epithelial to mesenchymal transition; limb development; middle ear morphogenesis; negative regulation of astrocyte differentiation; negative regulation of BMP signaling pathway; negative regulation of cardiac muscle cell proliferation; negative regulation of cell migration; negative regulation of osteoblast differentiation; negative regulation of transcription from RNA polymerase II promoter; nervous system development; osteoblast differentiation; skeletal development; somatic stem cell maintenance; wound healing

Disease: Brachydactyly, Type B2; Multiple Synostoses Syndrome 1; Stapes Ankylosis With Broad Thumb And Toes; Symphalangism, Proximal, 1a; Tarsal-carpal Coalition Syndrome