A disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains corresponding to Noggin Source: E. coli
Uniprot ID: P97466
Amino Acid Sequence: MQHYLHIRPA PSDNLPLVDL IEHPDPIFDP KEKDLNETLL RSLLGGHYDP GFMATSPPED RPGGGGGPAG GAEDLAELDQ LLRQRPSGAM PSEIKGLEFS EGLAQGKKQR LSKKLRRKLQ MWLWSQTFCP VLYAWNDLGS RFWPRYVKVG SCFSKRSCSV PEGMVCKPSK SVHLTVLRWR CQRRGGQRCG WIPIQYPIIS ECKCSC 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.
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 2 ng/ml, corresponding to a specific activity of > 5.0 x 10^5 IU/mg in the presence of 5 ng/ml BMP-4
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
NOG
Purity
>95%, by SDS-PAGE and HPLC
Endotoxin Note
Less than 1 EU/ug of Noggin as determined by LAL method.
Applications/Dilutions
Dilutions
Bioactivity
SDS-Page
Theoretical MW
46.4 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.
Store at -20 to -70C as supplied. After reconstitution, store at 2 to 8C for 1 month and at -20 to -70C for long term storage. Avoid repeated freeze-thaw cycles.
Buffer
Lyophilized from a 0.2 um filtered concentrated solution in 30 % acetonitrile, 0.1 % TFA.
Preservative
No Preservative
Concentration
LYOPH
Purity
>95%, by SDS-PAGE and HPLC
Reconstitution Instructions
Recommended to centrifuge prior to opening. Reconstitute in 10 mM HAc to a concentration less than 0.25mg/mL. Apportion stock solutions into working aliquots and store at <-20C.
Alternate Names for Recombinant Mouse Noggin Protein
NOG
Noggin
SYM1
symphalangism 1 (proximal)
synostoses (multiple) syndrome 1
SYNS1
SYNS1A
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 mouse Noggin shares 99% and 83% a.a. sequence identity with human and Xenopus 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 3 months from date of receipt.
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