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| Alternative Names | NOG, Noggin, SYM1, symphalangism 1 (proximal), synostoses (multiple) syndrome 1, SYNS1, SYNS1A |
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| Expression System | |
| Formulation | |
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Background
MULTIPLE is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: NOG, Noggin, SYM1, symphalangism 1 (proximal), synostoses (multiple) syndrome 1, SYNS1, SYNS1A.
Species origin: Human.
Noggin is a 46.2 kDa bioactive protein, which exists as a disulfide-linked homodimer (each chain 23.1 kDa). Noggin binds members of the transforming Growth Factors-beta (TGF beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP-4), which inactivates their activities. As a extracellular antagonist of BMP proteins, Noggin involves in the development of many body tissues, including nerve tissue, muscles, and bones. In addition, Noggin is able to inhibit chondrocyte differentiation through its interaction with GDF5.
Endotoxin:<0.1 EU per 1 μg of the protein by the LAL method.
Biological significance and function
MULTIPLE is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as Metabolism & Enzymology.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Source species: Human
- Molecular weight: The protein has a calculated MW of 49.11 kDa. The protein migrates as 27 kDa under reducing condition (SDS-PAGE analysis).
- Protein length: The secreted Human Noggin consists of 205 amino acids and has a predicted molecular mass of 27 kDa
- Expression region: Amino acid sequence derived from Human Noggin (Gln28-Cys232) (NP_005441.1) was expressed with 6×His tag at the C-terminus
- Purity: >98% as determined by SDS-PAGE.
- Biological activity: Measure by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 cells.The ED₅₀ for this effect is <0.05 μg/mL in the presence of 50 ng/mL of recombinant Human Noggin .
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.
Expression and purification strategy
Expression system: E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: His tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: The protein was lyophilized from a 0.2 µm filtered solution containing 1X PBS, pH 7.4. If you have any concerns or special requirements, please confirm with us.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.
What is the purity of Human Noggin protein, His tag (Animal-Free) (Human)?
What buffer is this protein supplied in?
How should Human Noggin protein, His tag (Animal-Free) (Human) be stored?
What expression system was used to produce this protein?
What is the molecular weight of this protein?
Is this protein biologically active?
What are the shipping conditions?
Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.