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Merck
CN

SRP3227

Sigma-Aldrich

NOGGIN from mouse

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

别名:

Mouse noggin, NOGGIN growth factor, NOGGIN protein

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关于此项目

UNSPSC代码:
12352202
NACRES:
NA.32
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生物来源

mouse

重组

expressed in E. coli

方案

≥98% (HPLC)
≥98% (SDS-PAGE)

表单

lyophilized

效能

1.0-2.0 ng/mL ED50

分子量

46.4 kDa

包装

pkg of 20 μg

技术

cell culture | mammalian: suitable

杂质

<0.1 EU/μg endotoxin, tested

颜色

white to off-white

UniProt登记号

运输

wet ice

储存温度

−20°C

基因信息

mouse ... NOG(18121)

一般描述

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.

应用

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.

生化/生理作用

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.

外形

Lyophilized with no additives.

制备说明

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.

其他说明

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

储存分类代码

13 - Non Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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分析证书(COA)

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Conditional inactivation of noggin in the postnatal skeleton causes osteopenia.
Canalis E, et al.
Endocrinology, 153(4), 1616-1626 (2012)
Noggin antagonizes BMP signaling to create a niche for adult neurogenesis.
Lim DA, et al.
Neuron, 28(3), 713-726 (2000)
David A Monteiro et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 35(3), e21263-e21263 (2021-02-12)
Bone is a dynamic tissue that constantly adapts to changing mechanical demands. The transforming growth factor beta (TGFβ) signaling pathway plays several important roles in maintaining skeletal homeostasis by both coupling the bone-forming and bone-resorbing activities of osteoblasts and osteoclasts
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)

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