Recombinant Human Neurosecretory Protein Vgf (VGF) Protein (His-GST&Myc)

Beta LifeScience SKU/CAT #: BLC-01030P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Neurosecretory Protein Vgf (VGF) Protein (His-GST&Myc)

Beta LifeScience SKU/CAT #: BLC-01030P
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Product Overview

Description Recombinant Human Neurosecretory Protein Vgf (VGF) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb O15240
Target Symbol VGF
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His-GST&C-Myc
Target Protein Sequence APPGRPEAQPPPLSSEHKEPVAGDAVPGPKDGSAPEVRGARNSEPQDEGELFQGVDPRALAAVLLQALDRPASPPAPSGSQQGPEEEAAEALLTETVRSQTHSLPAPESPEPAAPPRPQTPENGPEASDPSEELEALASLLQELRDFSPSSAKRQQETAAAETETRTHTLTRVNLESPGPERVW
Expression Range 23-206aa
Protein Length Partial
Mol. Weight 54.6 kDa
Research Area Neuroscience
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 Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner. VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning, memory, depression and chronic pain.; Plays a role in the control of body fluid homeostasis by regulating vasopressin release. Suppresses presynaptic glutamatergic neurons connected to vasopressin neurons.; Plays a role in the control of body fluid homeostasis by regulating vasopressin release. Activates GABAergic interneurons which are inhibitory neurons of the nervous system and thereby suppresses presynaptic glutamatergic neurons. Stimulates also feeding behavior in an orexin-dependent manner in the hypothalamus. Functions as a positive regulator for the activation of orexin neurons resulting in elevated gastric acid secretion and gastric emptying.; Secreted multifunctional neuropeptide that binds to different cell receptors and thereby plays multiple physiological roles including modulation of energy expenditure, pain, response to stress, gastric regulation, glucose homeostasis as well as lipolysis. Activates the G-protein-coupled receptor C3AR1 via a folding-upon-binding mechanism leading to enhanced lipolysis in adipocytes. Interacts with C1QBP receptor in macrophages and microglia causing increased levels of intracellular calcium and hypersensitivity.; Plays a role in the regulation of memory formation and depression-related behaviors potentially by influencing synaptic plasticity and neurogenesis. Induces acute and transient activation of the NTRK2/TRKB receptor and subsequent CREB phosphorylation. Induces also insulin secretion in insulinoma cells by increasing intracellular calcium mobilization.; Has bactericidal activity against M. luteus, and antifungal activity against P. Pastoris.
Subcellular Location [Neurosecretory protein VGF]: Secreted. Cytoplasmic vesicle, secretory vesicle. Note=Stored in secretory vesicles and then secreted, NERP peptides colocalize with vasopressin in the storage granules of hypothalamus.
Database References

HGNC: 12684

OMIM: 602186

KEGG: hsa:7425

STRING: 9606.ENSP00000249330

UniGene: PMID: 29209432

  • results suggest VGF enhances dendritic maturation and that these effects can be altered by common SNPs in the VGF gene PMID: 28287464
  • We conclude that some of the already identified variants in VGF from human polymorphism studies may contribute to eating disorders and obesity. PMID: 27088090
  • Data show although no any significant differences between patient groups and lean subjects of proteins SYT4, BAG3, APOA1, and VAV3, except for VGF protein, there was a trend between the expression of these four genes and their protein levels. PMID: 26337083
  • Data show that two VGF peptides (NAPP-19 and QQET-30) were identified in plasma. PMID: 26562304
  • Data indicate an increased number of neurosecretory protein VGF-expressing T cells in patients with Alzheimer's disease (AD) compared to aged healthy controls. PMID: 26142708
  • Results indicate that neuron-restrictive silencer factor plays an important role as a repressor of VGF gene regulation in neuroblastoma cells through a mechanism that is dependent on VGF-neuron-restrictive silencer element PMID: 25569790
  • NERPs may be potent endogenous suppressors of glucose-dependent insulin secretion. PMID: 25529453
  • DISC1 knockdown leads to a reduction of VGF in neurons. PMID: 24934694
  • Knock-in mice expressing human VGF were fertile, had increased body weight, whereas those with c-terminal region deletion had reduced adiposity, increased energy expenditure, and improved glucose tolerance. PMID: 25675362
  • We conclude that VGF contributes to survival and function of peripheral T cells PMID: 25013207
  • Among the 19 genes tested, VGF was found to be completely methylated in several Urothelial Cell Carcinoma cell lines PMID: 24830820
  • The expression of NPY and VGF was increased in the arcuate nucleus, but decreased in the nucleus of the Tractus Solitarius in the brains of type-II diabetic patients. PMID: 22808091
  • [review] The vgf gene is induced in vivo by neurotrophins including nerve growth factor (NGF), brain derived growth factor (BDNF) and glial derived growth actor (GDNF), by synaptic activity and by homeostatic and other stimuli. PMID: 21621608
  • VGF is regulated by SOD1 and plays a critical role in motor neuron survival PMID: 21151573
  • localization of neuroendocrine regulatory peptide-1 and-2 (NERP-1 and NERP-2); results suggest that neuroendocrine NERP-1 and NERP-2 might function as local modulatorsin the neuroendocrine system PMID: 20471433
  • VGF is downregulated in bipolar disorder in the CA region of the hippocampus and Brodmann's area 9 of the prefrontal cortex. PMID: 20631166
  • VGF mRNA levels were significantly reduced in drug-free depressed patients, as compared with controls, and were modulated in response to effective antidepressant treatment. PMID: 20164831
  • Application of neurosecretory protein VGF biomarker model to current diagnostic criteria provides an objective biomarker pattern that identifies patients with amyotrophic lateral sclerosis. PMID: 16481598
  • proVGF-related peptides are present in endocrine cells early during development and adulthood and increase in hyperplasia and tumors PMID: 17440014
  • while Vgf may be a reliable biomarker of progression of muscle weakness in patients with ALS, restoration of Vgf expression in spinal cord motor neurons may therapeutically rescue spinal cord motorneurons against excitotoxic injury PMID: 18432310
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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.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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