Noggin Human, Sf9

Noggin Human, Sf9

Growth Factors

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Description

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  • Name :

    Noggin Human, Sf9

    Description:

    Noggin Human Recombinant, Sf9

    SYM1, SYNS1, NOG.

    Product # :

    CYT-1119

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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  • description
  • source
  • formulation
  • purity
  • biological activity
  • More Info

Description

Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC
(b) Analysis by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.

More Info

  • Introduction

    Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

  • Synonyms

    SYM1, SYNS1, NOG.

  • Physical Appearance

    Sterile Filtered White lyophilized (freeze-dried) powder.

  • Stability

    Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

  • Solubility

    It is recommended to reconstitute the lyophilized Noggin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

  • Amino Acid Sequence

    QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Noggin Protein

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Frequently asked questions

1. Which company offers Recombinant Growth Factors at competitive prices?

ProSpec offers vast array of Growth Factors such as EGF| IGF1 | Leptin| VEGF and much more at affordable descent prices to meet academic budgets
ProSpec provides High Purity Growth Factors for 30 years, purity exhibits 95% and more as visualized by SDS-PAGE gel.
Growth Factors are in stock for immediate delivery via FedEx which enables scientists and researchers to perform immediate experiments.
Growth Factors are shipped globally using ProSpec’s custom tailored Styrofoam insulated box and premium ice packs that ensure maximum protein stability during transit to your laboratory.

2. Where can i find biologically active Growth Factors?

ProSpec offers biologically functional Growth Factors such as Prolactin | Erythropoietin | PDGF-BB which are rigorously tested in-vitro to provide researchers world wide BioActive Growth Factors.

3. What is the activity validation method for Growth Factors?

ProSpec uses cell-based bioassays that measures the biological activity, for example:
Activin-A is validated by Activin-responsive luciferase assay, SMAD2/3 phosphorylation.
CSF, G-CSF, GM-CSF, M-CSF are validated by Cytokine-dependent cell proliferation assay.
CTGF is validated by Fibroblast proliferation or migration assay.
EGF is validated by NIH3T3 or Balb/3T3 proliferation assay.
Epigen (EPGN) is validated by EGFR activation assay, cell proliferation.
Erythropoietin (EPO) is validated by TF-1 or UT-7 erythroid cell proliferation assay.
Fibroblast Growth Factors is validated by NIH3T3 proliferation assay.
IGF-1 and IGF-2 are validated by Cell proliferation assay (MCF-7, Saos-2, BALB/3T3).

4. Is the Growth Factor full length or partial?

The Growth Factor proteins are both full length and partial while majority of them are active mature proteins rather than a full-length precursor. ProSpec active mature proteins exhibits higher expression yields, better stability, Easier purification and equivalent biological activity as full length precursor.

5. Is the Growth Factor monomeric or dimeric form?

This depends on the Growth Factor. ProSpec Growth Factors are supplied in the native biologically active oligomeric state, which can be monomeric, dimeric, trimeric, or even multimeric since because receptor binding and biological activity often depend on correct oligomerization.
The EGF, Epigen, Fibroblast Growth Factors (FGF1, FGF2, FGF7/KGF)
HDGF, IGFBPs (IGFBP-1 to IGFBP-7), IGF2 are usually provided as monomer proteins though Activin-A and myostatin are supplied as homodimers.

6. What is the Growth Factor purity and how was it determined?

The Growth Factors purity ranges from high purity of ≥95% to premium grade ≥97%.
ProSpec uses SDS-PAGE Coomassie Blue Staining as the primary purity method which Visualizes protein bands. Some SDS-PAGE gels are stained with Silver Stain. Other analytical methods include RP-HPLC [ High-resolution purity determination ] , SEC-HPLC for the detections of aggregates and fragments and Western Blot to confirm Growth Factors identity.

7. Is the Growth Factor sequence verified?

The amino acid sequence verification is performed at DNA & protein level.
Sanger DNA Sequencing verifies the expression plasmid having correct coding.
LC-MS is used to verify the molecular weight of the final purified Growth Factor
Prospec also uses Edman N-terminal Sequencing to determine the amino-terminal sequence.

8. What is the endotoxin level in Growth Factors and how do you test LPS ?

ProSpec Growth Factors are tested for endotoxin also named LPS [ lipopolysaccharide ] which is found in the outer membrane of Gram-negative bacteria which can affect cytokine secretion, cell proliferation and stem cell.
ProSpec measures endotoxin using the Limulus Amebocyte Lysate [ LAL ] assay such as Gel-Clot.
ProSpec standard Endotoxin level for cytokines is usually <1 EU/ug.
What Does "EU" Mean? EU = Endotoxin Units

9. Is there host cell protein contamination?

There might be a minor existence of host-cell proteins post chromatography purification and quality-control procedures that greatly minimize these impurities. ProSpec tests host-cell protein levels by SDS-PAGE silver staining, or mass spectrometry.

10. Is the protein tested in vitro, in-vivo cell culture, stem cells, T cells, ELISA, western blot?

PoSpec Proteins are usually tested for biological activity and identity, while some proteins are not though supported by literature and customer experience. Interleukins are tested in T-cell, NK-cell, PBMC, stem cell culture. Interferons are tested in Antiviral assays, immune-cell activation, TNFA proteins are tested in Apoptosis, inflammation and immune studies. ProSpec does not conduct in-vivo or animal injections experiments in house or our source.