Recombinant Human Noggin Protein

Name: Recombinant Human Noggin Protein
Brand: Beta LifeScience
SKU: BL-2253NP
Availability: InStock

BL-2253NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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Product Overview

Description	Recombinant Human Noggin is produced by our Mammalian expression system and the target gene encoding Gln28-Cys232 is expressed.
Accession	Q13253
Synonym	Noggin; NOG
Gene Background	Noggin is a secreted homodimeric glycoprotein that is an antagonist of bone morphogenetic proteins (BMPs). Mature Human Noggin contains an N-terminal acidic region, a central basic heparin-binding segment and a C-terminal cysteine-knot structure. Noggin is very highly conserved among vertebrates, such that mature human Noggin shares 99%, 99%, 98%, 97% and 89% aa sequence identity with mouse, rat bovine, equine and chicken Noggin, respectively. Secreted Noggin probably remains close to the cell surface due to its binding of heparin-containing proteoglycans. Noggin binds some BMPs such as BMP4 with high affinity and others such as BMP7 with lower affinity. It antagonizes BMP bioactivities by blocking epitopes on BMPs that are needed for binding to both type I and type II receptors. Noggin is expressed in defined areas of the adult central nervous system and peripheral tissues such as lung, skeletal muscle and skin. During culture of human embryonic stem cells (hESC) or neural stem cells under certain conditions, addition of Noggin to antagonize BMP activity may allow stem cells to proliferate while maintaining their undifferentiated state, or alternatively, to differentiate into dopaminergic neurons.
Molecular Mass	23 KDa
Apmol Mass	25-33 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 500mM NaCl, 2mM EDTA, pH 7.4.
Endotoxin	Less than 0.01 EU/µg as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Biologically active. Please contact us to obtain bioactivity data.
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Essential for cartilage morphogenesis and joint formation. Inhibits chondrocyte differentiation through its interaction with GDF5 and, probably, GDF6.
Subcellular Location	Secreted.
Protein Families	Noggin family
Database References	HGNC: 7866 OMIM: 184460 KEGG: hsa:9241 STRING: 9606.ENSP00000328181 UniGene: PMID: 28981962 Report of a novel missense NOG mutation and phenotypic variability in an Indian family where multiple members were affected with tarsal-carpal coalition syndrome with multiple synostoses and proximal symphalangism. PMID: 29159868 Study suggested that the NOGGIN rs227731 polymorphism may increase nonsyndromic cleft lip with or without palate risk in Caucasians and may have no significant association in the Chinese population (meta-analysis). PMID: 28398705 The clinical presentation of the reported mutation corresponds with previous case reports of families with NOG mutation. In this family, surgery with stapedectomy had lasting effect without renewed fixation of the stapes in a follow up period of 18 months-38 years. PMID: 29605356 we describe a Danish family suffering from SYNS1 due to a novel NOG gene mutation (C230Y). We provide detailed clinical description of the family members presenting rare phenotype of the shoulders shared by affected individuals but no hearing loss, further adding to the phenotypic variability of the syndrome. PMID: 26994744 A New Subtype of Multiple Synostoses Syndrome Is Caused by a Mutation in GDF6 That Decreases Its Sensitivity to Noggin and Enhances Its Potency as a BMP Signal. PMID: 26643732 An imbalance between BMP-2 and Noggin secretion induces abnormal osteogenic differentiation of ankylosing spondylitis-mesenchymal stem cells. PMID: 26413886 early noggin exposure may play a specific role in the directed differentiation of DA cells from human embryonic stem cells. PMID: 26383864 By next-generation and Sanger sequencing analyses, study identified two novel mutations, c.559C>G (p.P178A) and c.682T>A (p.C228S), in the proximal symphalangism and atypical multiple synostosis syndrome families, respectively. PMID: 25391606 Novel p.W150C NOG mutation associated with proximal symphalangism and conductive hearing impairment was identified in a Chinese family.Impaired dimerization of mutant NOG is an important pathogenic mechanism for the NOG-related disorder. PMID: 25888563 No association between SPRY2, single-nucleotide polymorphisms, and nonsyndromic cleft lip with or without cleft palate risk were observed in this cohort of patients. PMID: 25339627 The study did not provide support for NOG being the causal gene at 17q22 in nonsyndromic cleft lip with or without cleft palate. PMID: 24706492 a novel NOG mutation in a Chinese family with proximal symphalangism PMID: 24326127 this study proposes that the decreased binding affinity of NOG with the p.R136C mutation to HSPG leads to an excess of bone morphogenetic protein signaling and underlies the proximal symphalangism and conductive hearing loss phenotype of carriers. PMID: 24735539 High-quality studies show that otosclerosis in Japanese patients is not linked to the NOG gene. [Review] PMID: 24170657 Even though gremlin 1 and noggin were not widely expressed in adult tissues, in a subset of organs their expression pattern indicated a potential role in normal tissue homeostasis as well as in malignancies. PMID: 23826422 A novel heterozygous change of p. R42T [c.C124A (CCC > ACC)] leading to a proline was identified in a family with multiple synostoses syndrome. PMID: 23732071 NOggin attenuates BMP4-mediated transdifferentiation of human valve interstitial cells towards an osteogenic-like phenotype in aortic valve sclerosis. PMID: 23483047 Mutations in the NOG gene are commonly found in congenital stapes ankylosis with symphalangism, but not in otosclerosis. PMID: 22288654 Noggin suppression decreased viability and BMP-2-induced osteogenic differentiation of human mesenchymal stem cells. PMID: 22740073 BMP2 treatment reduced noggin expression, which resulted in increased expression of apoptotic markers and increased apoptosis of osteoblasts. PMID: 22628200 high BMP6 activity, defined by strong BMP6 expression with weak noggin or SOST expression, was associated with shorter survival in esophageal SCC patients; results suggest BMP6, noggin and SOST could be used in combination as a prognostic indicator in cancer progression PMID: 22364398 p.G92E represents a rare polymorphism of the NOGGIN gene-- causing neither brachydactyly nor fibrodysplasia ossificans progressiva. PMID: 22529972 Human squamous cell carcinomas and malignant melanomas contain significantly more Myo/Nog cells than basal cell carcinomas. PMID: 22621191 we conclude that mutations in the coding region of NOG are rare, and play at most an uncommon role in human Holoprosencephaly (HPE). PMID: 22503063 Using genetic approaches, we show that when NOG is expressed in human breast cancer cells, it facilitates bone colonization by fostering osteoclast differentiation and bone degradation and also contributes to metastatic lesions reinitiation. PMID: 22547073 SNPs in the coding region of the NOG gene are identified infrequently in human cases of EA/TEF PMID: 22083168 evidence for a model of osteolytic bone metastasis where constitutive secretion of noggin by cancer cells mediates inhibition of bone formation, thereby preventing repair of osteolytic lesions generated by an excess of osteoclast-mediated bone resorption. PMID: 21249149 secreted levels of noggin were decreased in untreated patients with relapsing-remitting Multiple sclerosis PMID: 21111488 study reports on a family with facioaudiosymphalangism syndrome with overgrowth due to a novel heterozygous NOG missense mutation (c.696C > G, p.Cys232Trp) PMID: 20503332 This result suggests that there may be population polymorphism, or markers that are seldom polymorphic for our population PMID: 20645637 Using BMP-6/7 chimeras, we identified lysine 60 as a key residue conferring noggin resistance within the BMP-6 protein. PMID: 20048150 This study showed that constitutive and orthotopic Noggin protein expression did not influence cell proliferation, down-regulated BMP-2 expression, and showed no effect on BMP receptor transcripts. PMID: 19692649 A novel NOG gene mutation giving rise to the (P35S) amino acid substitution has been identified in an Italian family with symphalangism. PMID: 11857750 Autosomal dominant stapes ankylosis with broad thumbs and toes, hyperopia, and skeletal anomalies is caused by heterozygous nonsense and frameshift mutations in NOG, the gene encoding noggin PMID: 12089654 crystal structure of the antagonist Noggin bound to BMP-7, which shows that Noggin inhibits BMP signalling by blocking the molecular interfaces of the binding epitopes for both type I and type II receptors PMID: 12478285 Nog gene is connected to stapes ankylosis. PMID: 12621334 Here, we show that the overexpression of human noggin, by acting to inhibit glial differentiation by subependymal progenitor cells, can potentiate adenoviral BDNF-mediated recruitment of new neurons to the adult rat neostriatum PMID: 14999064 Mutations in the nog gene have been identified. PMID: 15264296 These studies highlight the critical role played by Cys168 in noggin's biological activities. PMID: 15756420 Overexpression of noggin in PC-3 cells inhibited the expansion of the lesion in vivo. PMID: 16126463 Data show calcium-sensing receptor stimulation of T-84 epithelia and colonic myofibroblasts downregulated the BMP family antagonist Noggin. PMID: 17138967 Lack of noggin expression by cancer cells may be a relevant mechanism contributing to the osteoblast response in bone metastases PMID: 17200191 Antagonism of bone morphogenetic protein signaling by transgenic Noggin plays a critical role in ensuring proper levels of cell proliferation and epithelial-to-mesenchymal transformation during cardiac morphogenesis. PMID: 17218603 Expression analysis of additional genes, AKT1, NOG and its antagonist BMP4, which interact downstream to FGFR1, demonstrated expression differences between primary rhabdomyosarcoma tumors and normal skeletal muscles PMID: 17696196 NOG is involved in myeloproliferative disease associated with myelofibrosis PMID: 17889703 Various mutations may occur in myositis ossificans nuclear families. PMID: 18019378 Heterozygous gene mutations in NOGGIN are associated with tall stature in children but not necessarily in adults. PMID: 18204269 Transgenic noggin overexpression increases the total number of neurons in the colon; the density of colonic neurons increases significantly in both Nog/+ and Nog/Nog mice, although the two groups of transgenic animals do not differ significantly. PMID: 18537141 Advanced melanoma cells may escape from BMP7-induced inhibition through concomitant aberrant expression of Noggin. PMID: 18560367

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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