Recombinant Mouse Noggin/NOG Protein, Active

Beta LifeScience SKU/CAT #: BEP-0050

Recombinant Mouse Noggin/NOG Protein, Active

Beta LifeScience SKU/CAT #: BEP-0050
/
Size

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Product Overview

Product Name Recombinant Mouse Noggin/NOG Protein
Target Symbol NOG
Alternative Names NOG, SYNS1, SYM1, Symphalangism 1 (proximal), SYNS1A, Synostoses (multiple) syndrome 1
Accession Number P97466
Expression System E. coli.
Molecular Weight 23 kDa (monomer, predicted)
Sequence Gln28-Cys232
Purity Determined by SDS-PAGE and quantitative densitometry by Coomassie® Blue staining
Activity Determined by in-house activity assay
Formulation Lyophilized from sterile PBS with Trehalose, pH 7.4
Endotoxin Level Available Upon Request
Shipping Shipped at ambient temperature.
Stability & Storage 12 months from date of receipt at -20°C to -70°C, lyophilized powder. 3 months at -20°C to -70°C under sterile conditions after reconstitution. Avoid repeated freeze-thaw cycles.
Reconstitution Reconstitute at 100 ug/mL in sterile PBS.
Target Function Noggin plays a crucial role in embryonic development and maintenance of various tissues. Its primary function is to inhibit the activity of bone morphogenetic proteins (BMPs) by directly binding to BMPs to block the interaction with the heteromeric BMP receptor complex. By inhibiting BMP signaling, Noggin helps to regulate processes such as cell differentiation, proliferation, and apoptosis (programmed cell death) during embryonic development. In particular, Noggin is involved in the formation of various structures in the embryo, including the central nervous system, limbs, and skeletal system. It helps to ensure proper patterning and growth of these structures by modulating BMP signaling gradients. Outside of embryonic development, Noggin also plays a role in tissue regeneration and repair in adults. In cell culture and organoid culture applications, Noggin maintains pluripotency and/or modulates differentiation.
Tissue Specificity During early embryonic development, Noggin is expressed in the embryonic ectoderm, including the neural tube, where it plays a critical role in regulating the formation and patterning of the central nervous system. Noggin continues to be expressed in the CNS throughout development and into adulthood. It is involved in regulating neural stem cell proliferation and differentiation and has been implicated in processes such as neurogenesis and synaptic plasticity. Noggin is expressed in the developing limb buds and developing skeletal tissues, including cartilage and bone, where it regulates bone formation and remodeling. Noggin expression has also been reported in other tissues and organs, including the kidneys, lungs, heart, and reproductive organs, where it may play various roles in development, homeostasis, and regeneration.
Cellular Localization Secreted protein
Involvement In Disease Dysregulation of Noggin has been implicated in the pathogenesis of osteoarthritis, skeletal dysplasias, fibrodysplasia ossificans progressiva (FOP), proximal symphalangism 1 (SYM1), multiple synostoses syndrome 1 (SYNS1) and neural tube defects.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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