Animal-Free Noggin Protein, Human (His)
Based on 1 Customer Validation
Noggin is an antagonist of bone morphogenetic proteins (BMPs) and a member of the TGF-β superfamily, existing as a homodimer. Noggin binds to BMP-2/-4/-7 and inhibits their binding to BMPR-I/II receptors, thereby synergistically inducing bone differentiation in HMSCs, maintaining pluripotency in hESCs, inhibiting angiogenesis in HUVECs, and promoting myelination in oligodendrocytes, exerting neural activity. Animal-Free Noggin Protein, Human (His) is an animal-free, recombinant human Noggin protein expressed in E. coli with a C-His tag. This product is recommended for use in cell culture.
- Species: Human
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
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Tel: 609-228-6898 E-mail: [email protected] [email protected]
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- References
- Help & FAQs
Biological Activity
Description
Noggin is an antagonist of bone morphogenetic proteins (BMPs) and a member of the TGF-β superfamily, existing as a homodimer. Noggin binds to BMP-2/-4/-7 and inhibits their binding to BMPR-I/II receptors, thereby synergistically inducing bone differentiation in HMSCs, maintaining pluripotency in hESCs, inhibiting angiogenesis in HUVECs, and promoting myelination in oligodendrocytes, exerting neural activity[1][2][3][4]. Animal-Free Noggin Protein, Human (His) is an animal-free, recombinant human Noggin protein expressed in E. coli with a C-His tag. This product is recommended for use in cell culture.
Background
1. Characteristics of Noggin
Noggin belongs to the TGF-β superfamily antagonist and belongs to the BMP binding protein family together with Chordin and Gremlin. It works through a secretory protein mechanism and is essential for normal bone development[1][5][6]. Noggin is a glycosylated homodimer linked by disulfide bonds and contains a conserved cysteine-knot domain. Noggin can specifically target ligands such as BMP-2, -4, and -7 and inhibit their binding to receptors[3]. It has a high affinity for hBMP-4 and a low affinity for hBMP-4. It is also an antagonist of hBMP-7[5]. Noggin binds to BMPs (such as BMP-2/-4) and blocks their interaction with type I (BMPR-IA/IB) and type II (BMPR-II) serine/threonine kinase receptors, inhibiting Smad1/5/8 phosphorylation and downstream transcription.
Noggin is involved in the regulation of bone differentiation: In human mesenchymal stem cells (HMSCs), Noggin synergizes with T cell inflammatory factor (TTII) or Dexamethasone (HY-14648) to induce alkaline phosphatase activity and mineralization, upregulates BMP-2 and osteocalcin expression, but does not affect Runx2[1].
Noggin is involved in the maintenance of stem cell pluripotency: In human embryonic stem cells (hESCs), it inhibits BMP4-induced differentiation, maintains the expression of pluripotency genes such as Oct4 and Nanog, and promotes cell proliferation[2].
Noggin inhibits angiogenesis: It blocks BMP-4 signaling in human umbilical vein endothelial cells (HUVEC), inhibits cell migration, tube formation and angiogenesis, and downregulates BMP-4 mRNA levels[3].
Noggin promotes nerve myelination: In oligodendrocyte differentiation, it relieves the inhibition of Sox10/Nkx2.2 by BMP, promotes Myelin Basic Protein (MBP) expression and myelination[4].
2. Application of Noggin
Noggin is used in combination with BMP to regulate the balance of osteoblast-osteoclast, which is used for bone defect repair and is suitable for bone tissue engineering[1]. Noggin also maintains the pluripotency of hESC, can optimize the differentiation of oligodendrocyte precursor cells, and is used in the study of myelin disease models such as multiple sclerosis[2]. Noggin also has anti-cancer activity by inhibiting endothelial cell migration and preventing tumor angiogenesis. Pretreatment of oligodendrocyte precursor cells with Noggin can enhance their myelination in BMP-deficient shiverer mice[4].
Verified Bioactivity
Measure by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 cells. The ED50 for this effect is <0.05 µg/mL in the presence of 50 ng/mL of recombinant human BMP-4.
Technical Parameters
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Species Human
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Source E. coli
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Tag C-6*His
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Accession
Q13253 (Q28-C232)
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Molecular Construction
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N-term
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Noggin (Q28-C232)
Accession # Q13253 -
6*His
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C-term
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Protein Length
Full Length of Mature Protein
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Synonyms
NOG; Symphalangism 1 (Proximal); Prev. SYNS1; SYNS1A; Prev. SYM1; Noggin; Synostoses (Multiple) Syndrome 1
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AA Sequence
QHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPPEDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGGQRCGWIPIQYPIISECKCSC
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Predicted Molecular Mass
24 kDa
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Molecular Weight
Approximately 27 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder
1.Lyophilized from a 0.22 μm filtered solution of 0.1% sarkosyl in PBS, pH 8.0, trehalose.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
Please refer to the lot-specific COA for specific buffer information.
<0.1 EU per 1 μg of the protein by the LAL method.
It is recommended to reconstitute to a concentration of 100-200 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (265 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
References
[1]. Rifas L. The role of noggin in human mesenchymal stem cell differentiation. J Cell Biochem. 2007 Mar 1;100(4):824-34. [Content Brief]
[2]. Chaturvedi G, et al. Noggin maintains pluripotency of human embryonic stem cells grown on Matrigel. Cell Prolif. 2009 Aug;42(4):425-33. [Content Brief]
[3]. Kang HW, et al. In vitro and In vivo imaging of antivasculogenesis induced by Noggin protein expression in human venous endothelial cells. FASEB J. 2009 Dec;23(12):4126-34. [Content Brief]
[4]. Izrael M, et al. Human oligodendrocytes derived from embryonic stem cells: Effect of noggin on phenotypic differentiation in vitro and on myelination in vivo. Mol Cell Neurosci. 2007 Mar;34(3):310-23. [Content Brief]
[5]. Groppe J, et al. Structural basis of BMP signalling inhibition by the cystine knot protein Noggin. Nature. 2002 Dec 12;420(6916):636-42. [Content Brief]
[6]. Brunet LJ, et al. Noggin, cartilage morphogenesis, and joint formation in the mammalian skeleton. Science. 1998 May 29;280(5368):1455-7. [Content Brief]
[7]. Miriyala S, et al. Bone morphogenic protein-4 induces hypertension in mice: role of noggin, vascular NADPH oxidases, and impaired vasorelaxation. Circulation. 2006 Jun 20;113(24):2818-25.Miriyala S, et al. Bone morphogenic protein-4 induces hypertension in mice: role of noggin, vascular NADPH oxidases, and impaired vasorelaxation. Circulation. 2006 Jun 20;113(24):2818-25. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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