Human Latent GDF-8 Protein 2039

$330.00 – $1,100.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Asn24-Ser375

SKU: 2039parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	O14793
express system	HEK293
product tag	N-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
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 41.19 kDa. Due to glycosylation, the protein migrates to 35-40 kDa and 45-55 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human Latent GDF-8 Protein 2039

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
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 at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
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

Data

The purity of Human Latent GDF-8 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human Latent GDF-8 Protein

Human Latent GDF-8 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.