SRP3227

Sigma-Aldrich

NOGGIN from mouse

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

NACRES:
NA.32
Pricing and availability is not currently available.

biological source

mouse

recombinant

expressed in E. coli

assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

potency

1.0-2.0 ng/mL ED50

mol wt

46.4 kDa

packaging

pkg of 20 μg

application(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white to off-white

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

mouse ... NOG(18121)

General description

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.

Biochem/physiol Actions

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.

Sequence

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

Physical form

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.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
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)
L J Brunet et al.
Science (New York, N.Y.), 280(5368), 1455-1457 (1998-06-20)
Noggin is a bone morphogenetic protein (BMP) antagonist expressed in Spemann's organizer. Murine Noggin is expressed in condensing cartilage and immature chondrocytes, as are many BMPs. In mice lacking Noggin, cartilage condensations initiated normally but developed hyperplasia, and initiation of...
The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4.
Zimmerman LB, et al.
Cell, 86(4), 599-606 (1996)
E Minina et al.
Development (Cambridge, England), 128(22), 4523-4534 (2001-11-21)
During endochondral ossification, two secreted signals, Indian hedgehog (Ihh) and parathyroid hormone-related protein (PTHrP), have been shown to form a negative feedback loop regulating the onset of hypertrophic differentiation of chondrocytes. Bone morphogenetic proteins (BMPs), another family of secreted factors...
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