Biotinylated Mouse Latent GDF-8 Protein (pro&latent)
Catalog No: GDF8-MB001
- Species
- Mouse
- Expression System
- HEK293
- Tag
- His, Avi
- Activity
- Activity verified
Product overview
Recombinant Biotinylated Mouse Latent GDF-8 Protein (pro&latent) is expressed in HEK293 cells with a His tag and Avi tag at the N-terminus. It contains amino acid residues Asn25-Ser376 (UniProt accession: O08689).
Product Details
- Molecular Aliases
- Myostatin; GDF8; Latent GDF8; Mstn;; Growth differentiation factor-8; Growth differentiation factor 8
- Protein Length
- Asn25-Ser376
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 42.99 kDa. Due to glycosylation, the protein migrates to 13-15 kDa, 38-40 kDa and 48-55 kDa based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE > 95% as determined by HPLC
- Endotoxin
- Less than 1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display
Biotinylated Mouse Latent GDF-8 (pro&latent) on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
The purity of Biotinylated Mouse Latent GDF-8 (pro&latent) is greater than 95% as determined by SEC-HPLC.
Immobilized Biotinylated Mouse Latent GDF-8, His Avi tag at 0.5μg/ml (100μl/well) on the streptavidin precoated plate (5μg/ml). Dose response curve for Apitegromab, hFc Tag with the EC50 of 4.8ng/ml determined by ELISA. (QC Test)
Background
Growth/differentiation factor 8 (GDF8), or myostatin, negatively regulates muscle mass. GDF8 is held in a latent state through interactions with its N-terminal prodomain. GDF8, like numerous TGF-β family members, is a disulfidelinked dimer that is synthesized as a precursor protein which requires cleavage by a furin-like protease to yield an N-terminal prodomain and a C-terminal mature, signaling domain.
References
- Walker RG, McCoy JC, Czepnik M, Mills MJ, Hagg A, Walton KL, Cotton TR, Hyvönen M, Lee RT, Gregorevic P, Harrison CA, Thompson TB. Molecular characterization of latent GDF8 reveals mechanisms of activation. Proc Natl Acad Sci U S A. 2018 Jan 30;115(5): E866-E875. doi: 10.1073/pnas.1714622115. Epub 2018 Jan 18. PMID: 29348202; PMCID: PMC5798348.
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