Reactivity | HuSpecies Glossary |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Recombinant
Human GDF-15
(Catalog # 8146-GD/CF)
binds to Recombinant Human GFR alpha -like
Fc Chimera (Catalog #
9697-GR)
with an ED50 of 0.0500-0.500 ng/mL. |
Source | Human embryonic kidney cell, HEK293-derived human GDF-15 protein Ala197-Ile308 |
Accession # | |
N-terminal Sequence | Ala197 |
Structure / Form | Disulfide-linked homodimer |
Protein/Peptide Type | Recombinant Proteins |
Gene | GDF15 |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
|
Theoretical MW | 12 kDa (monomer). 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. |
SDS-PAGE | 12-14 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in HCl. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 250 μg/mL in 4 mM HCl. |
Growth Differentiation Factor 15 (GDF-15), also called Macrophage Inhibitory Cytokine 1 (MIC-1), Placental Transforming Growth Factor beta , Prostate-derived Factor, and Placental Bone Morphogenetic Protein, is a divergent member of the Transforming Growth Factor beta (TGF-beta ) superfamily (1, 2). Human GDF-15 shares 66% and 68% amino acid sequence identity with the rat and mouse proteins, respectively (3). GDF-15 is highly expressed in placenta and brain, and it is expressed at lower levels in kidney, pancreas, prostate, and colon. Similar to other TGF-beta family proteins, GDF-15 is synthesized as a large precursor protein that is cleaved at a dibasic cleavage site (RxxR) to release the mature protein. The C-terminal domain of GDF-15 contains seven characteristic conserved cysteine residues necessary for the formation of the cysteine knot and the single inter-chain disulfide bond (4, 5). Biologically active GDF-15 is a disulfide-linked homodimer of the mature protein. GDF‑15 has been shown to have various functions, including inhibition of Tumor Necrosis Factor alpha (TNF-alpha ) production from lipopolysaccharide-stimulated macrophages and the induction of cartilage formation (1, 6). GDF-15 also promotes neuronal survival, and hypothalamic expression of GDF-15 causes appetite suppression via modulation of neuropeptide Y and pro-opiomelanocortin levels (7-10). GDF-15 is cardioprotective via inhibition of platelet activation, limiting atherosclerosis, promoting recovery following myocardial infarction, and regulating angiogenesis (11-15). Exposure of cardiomyocytes to GDF-15 results in Smad2 and Smad3 phosphorylation (16).
Taking Biomarker Discovery From 2D to 3D: Increased Biological Activity of EVs Isolated From 3D Prostate Cancer Cultures Jamshed Arslan, Pharm D, PhD Tissues within the human body are made of a three-dimensional (3D) arrangement of cells working together to perform vital functions. The commonly used 2D monolayer cultures have limited ... Read full blog post. |
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