Recombinant Mouse Growth/Differentiation Factor 15 (GDF15) Protein (His-SUMO)

Name: Recombinant Mouse Growth/Differentiation Factor 15 (GDF15) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-07156P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Growth/Differentiation Factor 15 (GDF15) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9Z0J7
Target Symbol	GDF15
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	SAHAHPRDSCPLGPGRCCHLETVQATLEDLGWSDWVLSPRQLQLSMCVGECPHLYRSANTHAQIKARLHGLQPDKVPAPCCVPSSYTPVVLMHRTDSGVSLQTYDDLVARGCHCA
Expression Range	189-303aa
Protein Length	Full Length of Mature Protein
Mol. Weight	25.5 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Binds to its receptor, GFRAL, and activates GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem. It then triggers the activation of neurons localized within the parabrachial nucleus and central amygdala, which constitutes part of the 'emergency circuit' that shapes feeding responses to stressful conditions. On hepatocytes, inhibits growth hormone signaling.
Subcellular Location	Secreted.
Protein Families	TGF-beta family
Database References	KEGG: mmu:23886 STRING: 10090.ENSMUSP00000003808 UniGene: PMID: 29491220 Membrane-protein extraction and use of an intracellular protein-transport inhibitor showed that GDF-15 promoted CaV3.1 and CaV3.3 alpha-subunit expression by trafficking to the membrane. PMID: 27353765 CHOP activates Gdf15 transcription via binding to its promoter upon endoplasmic reticulum stress. PMID: 28847729 The ANT1-deficient muscle mitochondria produce excess reactive oxygen species (ROS) and are partially uncoupled. Hence, the muscle respiration under nonphosphorylating conditions is increased. Muscle transcriptome analysis revealed the induction of mitochondrial biogenesis, down-regulation of diabetes-related genes, and increased expression of the genes encoding the myokines FGF21 and GDF15. PMID: 28223503 isolating GFRAL as the receptor for GDF15-induced anorexia and weight loss, the identification of a mechanistic basis for the non-homeostatic regulation of neural circuitry by a peripheral signal associated with tissue damage and stress; findings provide opportunities to develop therapeutic agents for the treatment of disorders with altered energy demand PMID: 28953886 These data suggest that GDF15 is required for IL-13-induced improvement of glucose intolerance in mice fed an HFD. PMID: 28874416 HIF-1alpha and GDF15 expression are inversely related under normoxia and hyperoxia. PMID: 28734801 This is the first study defining the role of Mic-1/Gdf15 in a number of behavioural domains. PMID: 28081177 epithelial restitution was promoted by enhanced NAG-1 expression and subsequent enterocyte locomotion during the early wound-healing process PMID: 27421482 GDF15 is a potent mitohormetic signal that safeguards against the onset of obesity and insulin resistance. PMID: 27986797 The aim of this study was to identify the role of endogenous Gdf-15 in the MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) mouse model of Parkinson's disease (PD) by comparing Gdf-15 (+/+) and Gdf-15 (-/-) mice. PMID: 27115420 The results of this study indicated the importance of Gdf-15 in promoting survival of DAergic neurons and regulating the inflammatory response post 6-OHDA lesion. PMID: 26733415 endogenous Growth/differentiation factor-15 is beneficial for axon regeneration following sciatic nerve crush PMID: 26077927 repeated cisterna magna administration of human umbilical cord blood-derived mesenchymal stem cells enhanced endogenous adult hippocampal neurogenesis and synaptic activity through a paracrine factor of GDF-15 PMID: 26154268 Levels of GDF-15 mRNA increased 2 h after induction of ventilator-induced lung injury in WT lungs. Non-hematopoietic cells are the main source of GDF-15. GDF-15 is required for platelet-leukocyte interactions during ventilator-induced lung injury. PMID: 25948320 hNAG-1 appears to be a novel therapeutic target in preventing and treating obesity and insulin resistance. PMID: 24531647 Collectively, hNAG-1 is an important regulator of mammalian longevity and may act as a survival factor. PMID: 25239873 Counterbalance between MIC-1 and ATF3 is critical for deciding the fate of enterocytes under the food chemical stress. PMID: 25180886 Growth differentiation factor 15, a marker of lung involvement in systemic sclerosis, is involved in fibrosis development but is not indispensable for fibrosis development. PMID: 24504814 Growth/differentiation factor 15 promotes EGFR signalling, and regulates proliferation and migration in the hippocampus of neonatal and young adult mice. PMID: 24496615 GDF-15 is therefore prominently upregulated in the retina after optic nerve crush but does not directly interfere with the magnitude and temporal progression of retinal ganglion cell death. PMID: 23640134 GDF15 protects the renal interstitium and tubular compartment in experimental type 1 and 2 diabetes without affecting glomerular damage PMID: 23986522 Enteropathogenic Escherichia coli enhances MIC-1 gene expression in the human intestinal cancer cells PMID: 23503457 knockdown of MIC-1 can decrease RNPC1-induced cell growth suppression. PMID: 23836903 This is the first study that demonstrates a protective role of GDF-15 in advanced atherosclerosis and macrophage accumulation, possibly due to the reduced expression of adhesion molecules. PMID: 23800095 MIC-1/GDF15 is involved in the physiological regulation of appetite and energy storage. PMID: 23468844 GDF-15 specifically inhibits platelet integrin activation, preventing thrombus formation. PMID: 23231375 GDF-15 is involved in orchestrating atherosclerotic lesion progression by regulating apoptotic cell death and IL-6-dependent inflammatory responses to vascular injury. PMID: 23316317 Increased expression of the TGF-b superfamily cytokine MIC-1/GDF15 protects ApoE(-/-) mice from the development of atherosclerosis. PMID: 22386250 GDF15 impairs aortic contractile and relaxing function through an endothelium-dependent mechanism involving altered caveolar endothelial NO synthase signaling. PMID: 23262134 MIC-1/GDF15 has complex actions on tumor behavior PMID: 22952779 identified the secreted protein follistatin-like 1 (FSTL1) as an inducer of GDF15 production. PMID: 22675198 The work shows that the molecule MIC-1/GDF15 might be beneficial for the treatment of obesity as well as perturbations in glucose homeostasis. PMID: 22514681 These findings suggest that GDF15 could play a pivotal role in the pathogenesis of bone loss relevant to hypoxia. PMID: 22190281 coronary artery ligation in Gdf15-deficient mice led to enhanced recruitment of polymorphonuclear leukocytes into the infarcted myocardium and an increased incidence of cardiac rupture PMID: 21516086 Regulation of GDF-15, a distant TGF-beta superfamily member, in a mouse model of cerebral ischemia. PMID: 21128084 GDF-15 deletion has a beneficial effect both in early and later atherosclerosis by inhibition of CCR2-mediated chemotaxis and by modulating cell death. PMID: 21242297 GDF-15 at endogenous levels contributes to proliferation and immune escape of malignant gliomas in an immunocompetent host. PMID: 20534737 Data show that MIC-1 is secreted from melanoma cells together with VEGF to promote vascular development mediated by (V600E)B-Raf signaling. PMID: 20431030 GDF-15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK PMID: 12514175 GDF-15/MIC-1 is an early mediator of the injury response in kidney and lung PMID: 15897808 GDF-15 induction is an immediate early response to liver injury that can occur through TNF and p53 independent pathways PMID: 16154591 GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance. PMID: 16397142 gdf15 is a growth factor with dual function either promoting proliferation or growth arrest and differentiation due most likely to differences in cellular differentiation PMID: 17286605 GDF-15 has no apparent effect on hepatocellular carcinoma (HCC) tumor formation rate, growth rate or invasiveness in diethylnitrosamine-induced HCC in vivo. PMID: 18210153 Data conclude that MIC-1 is expressed in adipose tissue and secreted from adipocytes and is therefore a new adipokine. MIC-1 may have a paracrine role in the modulation of adipose tissue function and body fat mass. PMID: 19074584 a possible inverse relationship exists between the expression of NAG-1 and COX-2 in tumor formation of colon tissue. PMID: 19375854 the NAG-1 protein inhibits urethane-induced tumor formation PMID: 19401523 Despite striking similarities in the GDF-15 and CNTF knock-out phenotypes, expression levels of CNTF and other neurotrophic factors in the sciatic nerve were unaltered suggesting that GDF-15 is a genuine novel trophic factor for motor and sensory neurons. PMID: 19864576

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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