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SRP3227

Sigma-Aldrich

NOGGIN from mouse

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Synonyme(s) :

Mouse noggin, NOGGIN growth factor, NOGGIN protein

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About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

mouse

Produit recombinant

expressed in E. coli

Pureté

≥98% (HPLC)
≥98% (SDS-PAGE)

Forme

lyophilized

Puissance

1.0-2.0 ng/mL ED50

Poids mol.

46.4 kDa

Conditionnement

pkg of 20 μg

Technique(s)

cell culture | mammalian: suitable

Impuretés

<0.1 EU/μg endotoxin, tested

Couleur

white to off-white

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

mouse ... NOG(18121)

Description générale

NOGGIN was first identified in the Xenopus embryos in an expression screen for activities that induce dorsal structures. It is a glycoprotein that is released as a homodimer. This protein is expressed during Xenopus gastrula stage. NOGGIN shows major expression in the central nervous system and is also expressed in lung, skin, skeletal muscle, cartilage, and bone. Recombinant murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Application

NOGGIN from mouse has been used as a supplement in the knockout serum replacement constituting the embryoid body medium containing DMEM/F-12. It has also been used as a supplement in PPC (photoreceptor progenitor cell) intermediate medium.

Actions biochimiques/physiologiques

NOGGIN proteins interact with BMPs (bone morphogenetic protein) and inhibit the activation of BMPRs. In Xenopus gastrula stage, NOGGIN is released by the Spemann organizer, and stimulates neural tissue from dorsal ectoderm by inhibiting ectodermal BMPs. In mouse embryo, this protein is not essential for neural induction, but is crucial for the later development of the neural tube, somite, and cartilage morphogenesis. Double homozygous mutant mice of NOGGIN and CHORDIN show prosencephalon developmental defects. In vitro it functions as a negative regulator of neuronal differentiation of neocortical precursors.
Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. Recombinant murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Séquence

MQHYLHIRPA PSDNLPLVDL IEHPDPIFDP KEKDLNETLL RSLLGGHYDP GFMATSPPED RPGGGGGPAG GAEDLAELDQ LLRQRPSGAM PSEIKGLEFS EGLAQGKKQR LSKKLRRKLQ MWLWSQTFCP VLYAWNDLGS RFWPRYVKVG SCFSKRSCSV PEGMVCKPSK SVHLTVLRWR CQRRGGQRCG WIPIQYPIIS ECKCSC

Forme physique

Lyophilized with no additives.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Jae-Hyun Kim et al.
Frontiers in pharmacology, 12, 690113-690113 (2021-08-06)
Fracture healing is related to osteogenic differentiation and mineralization. Recently, due to the unwanted side effects and clinical limitations of existing treatments, various natural product-based chemical studies have been actively conducted. Albiflorin is a major ingredient in Paeonia lactiflora, and
Noggin antagonizes BMP signaling to create a niche for adult neurogenesis.
Lim DA, et al.
Neuron, 28(3), 713-726 (2000)
Conditional inactivation of noggin in the postnatal skeleton causes osteopenia.
Canalis E, et al.
Endocrinology, 153(4), 1616-1626 (2012)
The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4.
Zimmerman LB, et al.
Cell, 86(4), 599-606 (1996)
Naren P Tallapragada et al.
Cell stem cell, 28(9), 1516-1532 (2021-04-30)
How stem cells self-organize to form structured tissues is an unsolved problem. Intestinal organoids offer a model of self-organization as they generate stem cell zones (SCZs) of typical size even without a spatially structured environment. Here we examine processes governing

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