Recombinant Human MANF Protein

Beta LifeScience SKU/CAT #: BL-1685SG

Recombinant Human MANF Protein

Beta LifeScience SKU/CAT #: BL-1685SG
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag N/A
Host Species Human
Accession P55145
Synonym Arginine-rich protein, Protein ARMET, ARP, Recombinant Human Mesencephalic Astrocyte-Derived Neurotrophic Factor (MANF)
Background MANF is a neurotrophic factor found mainly in central nervous tissues where it may remain localized to the endoplasmic reticulum/Golgi apparatus, or secreted. It has been shown that MANF plays an important role in protecting cells against tunicamycin and thapsigargin -induced cell death. Without MANF, cells become increasingly vulnerable to the aforementioned drugs. Also, MANF is structurally homologous to CDNF.
Description Recombinant Human MANF was produced in E. coli. This protein is purified with our unique purification methods.
Source E.coli
Molecular Weight 18.4 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human MANF Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. Following secretion by the ER/SR, directly binds to 3-O-sulfogalactosylceramide, a lipid sulfatide in the outer cell membrane of target cells. Sulfatide binding promotes its cellular uptake by endocytosis, and is required for its role in alleviating ER stress and cell toxicity under hypoxic and ER stress conditions.
Subcellular Location Secreted. Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen.
Protein Families ARMET family
Database References

Gene Functions References

  1. Our data indicate that increased MANF concentrations in serum are associated with the clinical manifestation of type 1 diabetes in children, but the exact mechanism behind the increase remains elusive PMID: 27356471
  2. Sulfatide binding promotes cellular MANF uptake and cytoprotection from hypoxia-induced cell death. PMID: 29497057
  3. Serum MANF level was higher in patients with newly diagnosed prediabetes and T2 Diabetes Mellitus than in normal glucose tolerance controls. MANF appears to be associated with Matsuda Index, QUICKI and HOMA-IR in prediabetes patients. PMID: 28216543
  4. the role of two short sequence motifs within the carboxy-(C) terminal domain of MANF in its neuroprotective activity, was studied. PMID: 26720341
  5. the selective expression of MANF in splenocytes may be involved in plasma cell differentiation and immune regulation. PMID: 26429332
  6. MANF is a protein that interacts with RTN1-C PMID: 25543119
  7. We demonstrate that Armet and Creld2 are genotype-specific ER stress response proteins with substrate specificities, and that aggregation of mutant matrilin-3 is a key disease trigger in MED that could be exploited as a potential therapeutic target PMID: 23956175
  8. MANF binding to the plasma membrane also required the RTDL sequence and was inhibited with a peptide known to interact with KDELRs, suggesting MANF binds KDELRs at the surface. PMID: 23255601
  9. MANF and C-MANF protect neurons intracellularly as efficiently as Ku70. PMID: 21047780
  10. Pretreatment with adeno-associated-virus vector containing human MANF reduces the volume of cerebral infarction and facilitates behavioral recovery in experimental stroke rats. PMID: 20685313
  11. Armet is a novel secreted mediator of the adaptive pathway of unfolded protein response. PMID: 18561914
  12. The widespread expression of MANF together with its evolutionary conserved nature and regulation by brain insults suggest that it has important functions both under normal and pathological conditions in many tissue types. PMID: 18718866
  13. structures of MANF and CDNF were solved; structure explains why MANF and CDNF are bifunctional; neurotrophic activity may reside in the N-terminal domain and ER stress response in the C-terminal domain PMID: 19258449

FAQs

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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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