Recombinant Human Metallothionein-3 (MT3) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-02227P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Metallothionein-3 (MT3) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-02227P
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.

Product Overview

Description Recombinant Human Metallothionein-3 (MT3) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P25713
Target Symbol MT3
Synonyms GIF; GIFB; GRIF; Growth inhibitory factor; Metallothionein 3 (growth inhibitory factor (neurotrophic)); Metallothionein 3; Metallothionein III; Metallothionein-3; Metallothionein-III; Mt 3; MT III; MT-3; MT-III; MT3; MT3_HUMAN; ZnMT3
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MDPETCPCPSGGSCTCADSCKCEGCKCTSCKKSCCSCCPAECEKCAKDCVCKGGEAAEAEAEKCSCCQ
Expression Range 1-68aa
Protein Length Full Length
Mol. Weight 33.9kDa
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 Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro.
Protein Families Metallothionein superfamily, Type 1 family
Database References
Tissue Specificity Abundant in a subset of astrocytes in the normal human brain, but greatly reduced in the Alzheimer disease (AD) brain.

Gene Functions References

  1. This study suggest that MT3 gene polymorphisms are not associated with autism. PMID: 29524106
  2. In recent years, the roles of zinc dynamics and MT3 function in neurodegeneration are slowly emerging. This short review focuses on the recent developments regarding the chemistry and biology of MT3. [review] PMID: 28538697
  3. C-terminal domain of MT3 confers dome formation in MCF-7 cells and the presence of this domain induces expression of the GAGE family of genes. The differential effects of MT3 and metallothionein 1E on the expression of GAGE genes suggests unique roles of these genes in the development and progression of breast cancer. PMID: 28545470
  4. The expression of MT-3 mRNA in breast cancer cell lines was significantly lower than in the normal human breast epithelial cell line. The results suggest that MT-3 may play a role in the malignant transformation of breast epithelial cells and in tumor progression. PMID: 27840910
  5. The epidermis of human skin and resulting malignancies express high level of MT-3. PMID: 25290577
  6. The study implicates the unique C-terminal sequence of MT-3 in the conversion of HK-2 cells to display an enhanced epithelial phenotype. PMID: 25803827
  7. MT3 may regulate breast cancer cell invasiveness by modulating the expression of MMP3. PMID: 25933064
  8. The presence of MT-3 in the zona glomerulosa of pathological adrenal cortex may imply a role in the pathophysiology of aldosterone-producing tissues. PMID: 24242700
  9. MT-capital I, Ukrainiancapital I, Ukrainiancapital I, Ukrainian increases the amount of active ADAM10 in association with furin, PC7 and PKCalpha. PMID: 24859040
  10. Upregulation of MT-3 gene expression can inhibit esophageal cancer cell proliferation and induce apoptosis. PMID: 24222235
  11. The experiments indicate that MT3 is an androgen-upregulated gene, and promotes tumorigenesis of prostate carcinoma cells. PMID: 23794209
  12. the molecular mechanism for protection against the neuronal cytotoxicity of Abeta(1-42) with copper ions PMID: 23086305
  13. MT-III expression may have an impact on the pathogenesis of non-small cell lung cancer. PMID: 23482768
  14. MT-3 modulates the catalytic redox properties of PrP-Cu(II) PMID: 22615124
  15. Esophageal adenocarcinomas are characterized by frequent epigenetic silencing of MT3. PMID: 21818286
  16. Metallothionein-III is a specific component of glial cytoplasmic inclusions and is upregulated in multiple system atrophy. PMID: 20039155
  17. The roles of zinc and metallothionein-3 in autophagy and/or lysosomal function are reviewed. PMID: 20974010
  18. MT-3 expression is involved in the transport function of a human renal cell line that retains properties of the proximal tubule. PMID: 11849386
  19. Overexpression of human metallothionein-III prevents hydrogen peroxide-induced oxidative stress in human fibroblasts. "metallothionein-III " PMID: 12067712
  20. overexpression can influence the growth and chemotherapeutic drug resistance of the PC-3 prostate cancer cell line PMID: 12111700
  21. Hypermethylation of metallothionein-3 CpG island in gastric carcinoma PMID: 12538345
  22. Metallothionein-III has anticarcinogenic and neuroprotective roles in cells exposed to gamma rays PMID: 15190073
  23. The affect the role of MT3 on cell viability, which may explain in part why the comprehensive effect of MT3 on the cells was elusive. PMID: 16087360
  24. analysis of the epitope of neuronal growth inhibitory factor (GIF) PMID: 16336778
  25. MT3 expression is frequently down-regulated in oesophageal squamous cell carcinoma , by DNA methylation, but that this is not a prognostic indicator PMID: 16351731
  26. mutation of MT3 at Glu23 may alter the NO metabolism and/or affect zinc homeostasis in brain, thus altering the neuronal growth inhibitory activity PMID: 16945328
  27. The alpha-domain is indispensable and plays an important role in modulating the stability of the metal cluster in the beta-domain by domain-domain interactions, thus influencing the bioactivity of hMT3. PMID: 17712581
  28. The level of MT-3 expression in human proximal tubular cells influences transepithelial resistance and cadherin expression but does not the Cd(+2)-induced loss of vectorial active transport. PMID: 18182399
  29. MT-3 is a highly hypoxia-inducible gene in human adipocytes; the protein may protect adipocytes from hypoxic damage PMID: 18206644
  30. These results suggest that MT-III upregulates VEGF production in brain endothelial cells by a HIF-1alpha-dependent mechanism. PMID: 18295594
  31. The structure adopted by the (6)CPCP(9) motif is the determinant factor of the inhibitory bioactivity of hGIF; but residues within the N-terminal fragment may also influence the peptide conformation and contribute to the protein's bioactivity. PMID: 18533104
  32. Metallothionein-III-induced activation of phosphatidylinositol 3-kinase/Akt and extracellular signal-regulated kinase1/2 up-regulates expression and activity of heme oxygenase-1, which provides protection against oxidative damage in dopaminergic cells. PMID: 18554677
  33. the bioactivity of hGIF is mainly related to the essential metal release and its characteristic conformation. PMID: 18757100
  34. metallothionein in decidual cells seems to be responsible for the proper coexistence between decidual cells and activated immune cells that infiltrate both eutopic and ectopic decidua during cesarean section and placental abruption PMID: 18782281
  35. In this study, the binding of Zn(2+), Ca(2+), and Mg(2+) to human Zn(7)MT-3 and its mutant lacking an acidic hexapeptide insert, Zn(7)MT-3(Delta55-60), was investigated and compared with the binding of Zn(7)MT-2. PMID: 19425569
  36. Results provide information on the domain-domain interaction at the molecular level, and shed new light on the mechanism of the bioactivity of human neuronal growth inhibitory factor. PMID: 19490120
  37. study of reaction/binding of cisplatin and transplatin with MT-3 and MT-2 initially bound with zinc; study includes kinetics and stoichiometry of the reactions PMID: 19536566
  38. weak in pancreatic serous cystadenomas; increased expressions in adenomocarcinomas; potential prognostic marker PMID: 19578815

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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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