Recombinant Human Noggin Protein (NBP2-35079)

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Human Noggin Protein [NBP2-35079]

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Func, PAGE
Format
CF
Concentration
LYOPH

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Catalog# & Formulation Size Price

Recombinant Human Noggin Protein Summary

Description
A biologically active protein to NOG.

Source: E. coli

Amino Acid Sequence: MQHYLHIRPA PSDNLPLVDL IEHPDPIFDP KEKDLNETLL RSLLGGHYDP GFMATSPPEDRPGGGGGAAG GAEDLAELDQ LLRQRPSGAM PSEIKGLEFS EGLAQGKKQRLSKKLRRKLQ MWLWSQTFCP VLYAWNDLGS RFWPRYVKVG SCFSKRSCSVPEGMVCKPSK SVHLTVLRWR CQRRGGQRCG WIPIQYPIIS ECKCSCPurity Specification:46.2kDa, >95%SDS-PAGE Results:25.5kDa, 81.8% ED50 Spec:3 ng/mLED50 Actual:0.872 ug/mLCells:ATDC-5
Preparation
Method
Novus' biologically active proteins are stringently purified to provide only the safest and most highly effective proteins available. This protein was expressed in E. coli, purified by HPLC, QC tested by SDS-PAGE and Western Blot and validated on appropriate cell lines for bioactivity. All HPLC and bioactivity data is provided for your assurance.
Details of Functionality
Noggin Protein is fully biologically active when compared to standard. The ED50 as determined by inhibiting BMP-4- induced alkaline phosphatase production of murine ATDC5 cells is less than 3.0 ng/ml, corresponding to a specific activity of > 3.3 x 105 IU/mg in the presence of 5 ng/ml rHuBMP-4.
Protein/Peptide Type
Biologically Active Protein
Gene
NOG
Purity
>95% pure by SDS-PAGE
Endotoxin Note
Less than 1 EU/ug of endotoxin as determined by LAL method.

Applications/Dilutions

Theoretical MW
46.3 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at 4C after rehydration. For extended storage after rehydration, add an equal volume of glycerol and store at -20C. Avoid repeated freeze-thaw cycles.
Buffer
Lyophilized from a 0.2 um filtered concentrated solution in 30 % acetonitrile, 0.1 % TFA.
Concentration
LYOPH
Purity
>95% pure by SDS-PAGE
Reconstitution Instructions
Reconstitute with 10 mM HAc to a final concentration of 0.1 - 1.0 mg/ml.

Notes

This lyophilized preparation is stable at 2-8 degrees C, but should be kept at -20 degrees C for long term storage, preferably desiccated. Upon reconstitution, the preparation is most stable at -20 to -80 degrees C, and can be stored for one week at 2-8 degrees C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 degrees C to -80 degrees C. Avoid repeated freeze/thaw cycles.

Alternate Names for Recombinant Human Noggin Protein

  • NOG
  • Noggin
  • SYM1
  • symphalangism 1 (proximal)
  • synostoses (multiple) syndrome 1
  • SYNS1

Background

Noggin encoded by the NOG gene, was first isolated from Xenopus, having the function of inducing secondary axis formation in frog embryos. It inhibits TGF- beta family ligands and preventing them from binding to their corresponding receptors. Noggin was originally found as a BMP-4 antagonist, and then has been shown to modulate the activities of other BMPs (BMP-2, 7, 13 and 14). Additionally, it has pleiotropic effect, both in early development and later stages. 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. In recent report, proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) have relation with the mutant of evolutionarily conserved amino acid residues of Noggin. Mature human Noggin shares 99 %, 99 %, 98 %, 97 % and 89 % a.a. sequence identity with mouse, rat, bovine, equine and chicken Noggin, respectively

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 2 years from date of receipt.

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Bioinformatics

Gene Symbol NOG
Entrez
Uniprot