Noggin Mouse

Noggin Mouse Recombinant
Cat. No.
BT24475
Source
Escherichia Coli.
Synonyms
Noggin, SYM1, SYNS1, NOG.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Noggin Mouse Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked protein consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.4 kDa (each chain 23.2 kDa).

Product Specs

Introduction
Noggin, a secreted polypeptide encoded by the NOG gene, plays a crucial role in embryonic development and bone formation. It inhibits signaling proteins in the transforming growth factor-beta (TGF-beta) superfamily, including bone morphogenetic protein-4 (BMP4). Noggin's ability to diffuse efficiently through extracellular matrices allows it to establish morphogenic gradients. This protein exhibits pleiotropic effects throughout development. Initially identified in Xenopus, noggin restored normal dorsal-ventral body axis in embryos with UV-induced ventralization. Mouse knockout studies underscore noggin's involvement in neural tube fusion, joint formation, and other developmental processes. Notably, dominant human NOG mutations are linked to proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1), both characterized by multiple joint fusions. These syndromes map to chromosome 17q22, the same region as NOG. Importantly, all NOG mutations affect evolutionarily conserved amino acid residues. Human noggin shares significant homology with its Xenopus, rat, and mouse counterparts.
Description
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).
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2µm filtered solution containing 30% acetonitrile and 0.1% TFA.
Solubility
Before opening, briefly centrifuge the product to collect contents at the bottom. Reconstitute in 10mM HAc to achieve a concentration of 0.1-1.0 mg/ml. For further dilutions, use appropriate buffered solutions.
Stability
Lyophilized Mouse Noggin remains stable at room temperature for 3 weeks. However, it is recommended to store desiccated below -18°C. Upon reconstitution, store Mouse Noggin at 4°C for 2-7 days or below -18°C for future use. For long-term storage, add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
Determined by SDS-PAGE, purity is greater than 95.0%.
Biological Activity
The ED50, determined by inhibiting BMP-4-induced alkaline phosphatase production in murine ATDC5 cells, is less than 2ng/ml. This translates to a specific activity exceeding 5.0 x 10^5 IU/mg in the presence of 5ng/ml BMP-4.
Synonyms
Noggin, SYM1, SYNS1, NOG.
Source
Escherichia Coli.
Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYD
PGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKG
LEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRF
WPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGQR
CGWIPIQYPIISECKCSC.

Product Science Overview

Structure and Function

Noggin is a disulfide-linked homodimer, meaning it consists of two identical subunits connected by disulfide bonds . It functions primarily as an antagonist to Bone Morphogenetic Proteins (BMPs), particularly BMP-4, but also modulates the activities of other BMPs such as BMP-2, BMP-7, BMP-13, and BMP-14 . By binding to these BMPs, Noggin prevents them from interacting with their receptors, thereby inhibiting their signaling pathways .

Role in Development

Noggin’s ability to inhibit BMP signaling is critical during embryonic development. It helps regulate the formation of the neural tube, somites, and other structures by controlling the balance between BMP signaling and other pathways. This balance is essential for proper tissue differentiation and organogenesis .

Recombinant Mouse Noggin

Recombinant Mouse Noggin is produced using a mouse myeloma cell line (NS0) and is typically purified to a high degree of purity (>90%) using SDS-PAGE under reducing conditions . The recombinant protein is often used in research to study its effects on cell differentiation, tissue culture, and various bioassays.

Applications

Recombinant Mouse Noggin is widely used in scientific research due to its ability to inhibit BMP-induced processes. Some of its applications include:

  • Cell Culture: Used to study the effects of BMP inhibition on various cell types.
  • Bioassays: Employed in assays to measure its ability to inhibit BMP-induced alkaline phosphatase production in chondrogenic cells .
  • Tissue Engineering: Investigated for its potential in promoting tissue regeneration and repair by modulating BMP signaling.
Storage and Stability

Recombinant Mouse Noggin is typically lyophilized and can be reconstituted in sterile PBS. It is stable for up to 12 months when stored at -20 to -70°C and for shorter periods at 2 to 8°C after reconstitution .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.