Noggin Human, HEK

Noggin Human Recombinant, HEK

This product consists of recombinant human Noggin, produced in HEK293 cells. It is a polypeptide chain with 211 amino acids (28-232a.a.) and a molecular mass of 23.8kDa. When analyzed using SDS-PAGE, the molecular size appears between 28-40kDa. The Noggin protein features a 6 amino acid His tag at the C-Terminus and is purified through proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT24298
Source

HEK293 Cells.

Appearance
A clear and colorless solution that has been sterilized by filtration.

Noggin Human, Sf9

Noggin Human Recombinant, Sf9

Produced in Sf9 insect cells using a baculovirus expression system, this recombinant Noggin is a glycosylated homodimer, composed of two identical subunits. Each subunit contains 205 amino acids, contributing to a total molecular mass of 47.9 kDa under non-reducing conditions. Notably, during SDS-PAGE analysis, the apparent molecular size may range from 50 to 80 kDa due to glycosylation. The purification process involves proprietary chromatographic techniques ensuring high purity.

Shipped with Ice Packs
Cat. No.
BT24402
Source

Sf9, Baculovirus cells.

Appearance

This product appears as a sterile, white powder obtained through lyophilization (freeze-drying).

Noggin Mouse

Noggin Mouse Recombinant

Recombinant Mouse Noggin, produced in E. coli, is a non-glycosylated protein with two polypeptide chains linked by disulfide bonds. Each chain comprises 206 amino acids, resulting in a total molecular weight of approximately 46.4 kDa (23.2 kDa per chain).
Shipped with Ice Packs
Cat. No.
BT24475
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Noggin Human

Noggin Human Recombinant

Recombinant human Noggin, produced in E. coli, is a non-glycosylated homodimer, meaning it consists of two identical protein chains. It lacks disulfide bonds and has a molecular weight of approximately 46.3 kDa. The protein is purified using advanced chromatographic methods to ensure its high quality and purity.
Shipped with Ice Packs
Cat. No.
BT24233
Source
Escherichia Coli.
Appearance
White, lyophilized (freeze-dried) powder, sterile filtered for purity.
Definition and Classification

Noggin, also known as NOG, is a protein encoded by the NOG gene in humans. It is a member of the cysteine knot superfamily and functions as an extracellular antagonist of bone morphogenetic proteins (BMPs). Noggin is highly conserved across species, including humans, mice, and Xenopus (an aquatic frog genus) .

Biological Properties

Key Biological Properties: Noggin is a secreted protein that plays a crucial role in vertebrate dorsoventral patterning. It binds and inhibits the activity of BMPs, particularly BMP2, BMP4, BMP5, BMP6, BMP7, BMP13, and BMP14 .

Expression Patterns and Tissue Distribution: Noggin is expressed in various tissues, including nerve tissue, muscles, and bones. It is released from the notochord and regulates BMP4 during development . Increased plasma levels of Noggin have been observed in obese mice and in patients with a body mass index over 27 .

Biological Functions

Primary Biological Functions: Noggin is essential for correct nervous system, somite, and skeletal development. It promotes somite patterning in the developing embryo and regulates the patterning of the neural tube and somites from the neural plate .

Role in Immune Responses and Pathogen Recognition: While Noggin’s primary functions are related to development, it also plays a role in learning, cognition, bone development, and neural tube fusion .

Modes of Action

Mechanisms with Other Molecules and Cells: Noggin binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as BMP4. By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, Noggin creates morphogenic gradients .

Binding Partners and Downstream Signaling Cascades: Noggin binds to BMPs via a conserved N-terminal clip domain, preventing BMP binding to type I and type II serine-threonine kinase receptors and inhibiting signaling mediated by Smad1/5/8 .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: Noggin’s expression and activity are tightly regulated during development. It is released from the notochord and regulates BMP4 during development . Noggin can also bind to ActivinB, Nodal/Xnrs, and XWnt8, inactivating these pathways to induce head formation in Xenopus embryos .

Transcriptional Regulation and Post-Translational Modifications: Noggin’s transcription is regulated by various factors during development, ensuring its precise expression in specific tissues .

Applications

Biomedical Research: Noggin is used in research to study its role in development and disease. It has been shown to have anti-cancer effects by inhibiting BMP activity .

Diagnostic Tools and Therapeutic Strategies: Noggin is explored for its potential in bone regenerative therapies. It promotes osteogenesis in human adipose-derived mesenchymal stem cells via FGFR2/Src/Akt and ERK signaling pathways . Noggin recombinant proteins are used in functional assays, ELISA, immunohistochemistry, and Western blot .

Role in the Life Cycle

Role Throughout the Life Cycle: Noggin is crucial during early embryonic development, particularly in neural induction and skeletal development. It continues to play a role in learning, cognition, and bone development throughout life . Noggin’s depletion in adipose tissue has been linked to obesity .

© Copyright 2024 Thebiotek. All Rights Reserved.