Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
target | Human/Mouse/Rat GDF-8 |
express system | HEK293 |
product tag | No Tag |
purity | > 95% as determined by Tris-Bis PAGE |
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. |
molecular weight | The protein has a predicted MW of 12.40 kDa. Due to glycosylation, the protein migrates to 13-15 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human/Mouse/Rat GDF-8 Protein 2000
$405.00 – $1,300.00
Summary
- Mammalian expression: HEK293
- Active: Yes
- Amino Acid Range: Asp267-Ser375
Human/Mouse/Rat GDF-8 Protein 2000
protein |
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Size and concentration 100, 500µg and liquid |
Form Liquid |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped with dry ice. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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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. |
Protein names Growth/differentiation factor 8 (GDF-8) (Myostatin) |
Gene names MSTN,MSTN GDF8 |
Protein family TGF-beta family |
Mass 9606Da |
Function Acts specifically as a negative regulator of skeletal muscle growth. |
Subellular location Secreted . |
Structure Homodimer; disulfide-linked (PubMed:27625211). Interacts with WFIKKN2, leading to inhibit its activity (PubMed:12595574). Interacts with FST3 (PubMed:17878677). |
Post-translational modification Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase. |
Target Relevance information above includes information from UniProt accession: O14793 |
The UniProt Consortium |
Publications
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