Recombinant Human Noggin Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications BA
Concentration
Lyoph

Order Details

Recombinant Human Noggin Protein Summary

Description
A recombinant protein corresponding to 206 amino acids of Human Noggin
Details of Functionality
Determined by its ability to inhibit 5 ng/ml of BMP-4-induced alkaline phosphatase production by ATDC chondrogenic cells. The expected ED50 for the effect is 0.05-0.08 ug/ml of Noggin
Source
E. coli
Protein/Peptide Type
Biologically Active Protein
Gene
NOG
Purity
>95%, by SDS-PAGE
Endotoxin Note
<0.1 ng/ug

Applications/Dilutions

Theoretical MW
23.1 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 -20 to -80C. Avoid freeze-thaw cycles.
Buffer
Sterile filtered and lyophilized with no additives
Concentration
Lyoph
Purity
>95%, by SDS-PAGE
Reconstitution Instructions
Reconstitute in H2O to a concentration of 0.1 to 1.0 mg/ml. Note: Due to solubility reasons the protein should be kept at low pH. This solution can then be diluted into other aqueous buffers

Alternate Names for Recombinant Human Noggin Protein

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

Background

Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-Beta family and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 23.1 kDa non-disulfide-linked homodimer consisting of a total of 206 amino acid residues.

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