Recombinant Human Metallothionein-1A (MT1A) Protein (GST)

Name: Recombinant Human Metallothionein-1A (MT1A) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08236P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Metallothionein-1A (MT1A) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P04731
Target Symbol	MT1A
Synonyms	CES 1; CES1; Metallothionein 1A; Metallothionein 1S; Metallothionein 2; Metallothionein 2A; Metallothionein IA; Metallothionein II; Metallothionein-1A; Metallothionein-IA; Metallothionein2; MGC32848; MT 1A; MT 2; MT 2A; MT IA; MT II; MT-1A; MT-IA; MT1; MT1A; MT1A_HUMAN; MT1S; MT2; MT2A; MTC
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MDPNCSCATGGSCTCTGSCKCKECKCTSCKKSCCSCCPMSCAKCAQGCICKGASEKCSC
Expression Range	1-59aa
Protein Length	Partial
Mol. Weight	32.9kDa
Research Area	Epigenetics And Nuclear Signaling
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.
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	Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Protein Families	Metallothionein superfamily, Type 1 family
Database References	HGNC: 7393 OMIM: 156350 KEGG: hsa:4489 STRING: 9606.ENSP00000290705 UniGene: Hs.655199

Gene Functions References

Full-length recombinant MT isoform 1a and it's isolated domain fragments were alkylated, changing protein conformation. PMID: 29518586
MT1A is aberrantly silenced by DNA methylation of 5' MT1A CpG island in melanoma. PMID: 28764861
Using a combination of electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and emission spectroscopy, this study reports that the Cu(i) to human apo-MT1A binding mechanism is highly pH-dependent. PMID: 28466911
Disruption of metallothionein I and II genes in mouse produced viable mice with increased susceptibility to cadmium poisoning. PMID: 8290567
Selective cysteine modification of metal-free human metallothionein 1a and its isolated domain fragments: Solution structural properties revealed via ESI-MS. PMID: 28187517
blockade of metallothioneins 1 and 2 constitutes a promising approach for the treatment of conditions which result in muscle atrophy. PMID: 27956698
Neonatal phthalate ester exposure induced placental MTs, FATP1 and HFABP mRNA expression PMID: 26867681
The present study was undertaken to explore further the interrelationship between p53 and metallothioneins. PMID: 27049123
MTF1 heads a hierarchy of zinc sensors, and through controlling the expression of a raft of metallothioneins and other key proteins involved in controlling intracellular zinc levels (e.g. ZnT1) alters zinc buffering capacity and total cellular zinc content. PMID: 26824222
These results clearly suggest that MT-1 may be involved in AD pathogenesis. PMID: 26836194
Zn(ii) and Cd(ii) metalation of the human MT1a takes place through two distinct pathways. PMID: 26583802
We report on the competitive zinc metalation of apo-carbonic anhydrase [CA; metal-free CA (apo-CA)] in the presence of apo-metallothionein 1A domain fragments to identify domain specific determinants of zinc binding and zinc donation PMID: 26475450
The Zinc and Cadmium exchange kinetics between human MT1A and carbonic anhydrase were examined using time-dependent electrospray ionization mass spectrometry. PMID: 26401817
Modeling of the reactions showed that at both physiological (7.4) and acidic (5.8) pHs, zinc binding and cadmium exchanges occur essentially randomly between two MT1A fragments. PMID: 26167879
Data indicate the calculated equilibrium zinc binding constants of each of the 7 zinc metallothionein 1A species ranged from a high of (log(KF)) 12.5 to a low of 11.8. PMID: 25208334
Low MT1A expression is associateed with lung carcinogenesis. PMID: 23947958
The metal-free, apo-alpha-MT also adopts a folded structure in the presence of the As(3+) even though there is no As(3+) bound. PMID: 24140052
Increased metallothionein expression reflects steroid resistance in renal allograft recipients. PMID: 23763497
Polymorphisms in the MT1A gene may influence excretion of urine uric acid and N-acetyl-beta-D-glucosamine in chronic lead-exposed workers. PMID: 23429061
MT-1A is epigenetically regulated by PU.1 during monocytic differentiation. PMID: 23501100
During the titration with Zn(2+), the electrospray ionization mass spectrometry data show that several metalated species coexist until the fully saturated proteins are formed. PMID: 23506369
MT1A rs11076161 was associated with B-Cd concentrations and Cd-induced kidney toxicity at high exposure levels. PMID: 22995156
A positive correlation between MT and Ki-67 expression was observed for all the studied cases but was even stronger in the metatypic subtype of basal cell carcinoma. PMID: 23042264
Variations in the ability of LAT1/DMT1/MTF1/MT1a to process and transport Hg may not play a significant role in the etiology of autism. PMID: 21798283
Possible role of MT as a marker of cell stress and homeostasis restoration in Graves'disease. PMID: 22090273
The expression of metallothioneins MT1A and MT1X was significantly downregulated during differentiation of Caco-2 cells treated with high levels of zinc. PMID: 21103883
MT-1A, -1F, -1G, -1X and -2A isoforms are significantly down-regulated in proliferating keloid fibroblasts. PMID: 20812968
Data show that MT-I + II and megalin are significantly altered in CNS lymphoma relative to controls. PMID: 20038220
Metallothionein, potential interaction partner for ECRG2, might be involved in regulation of cell proliferation and apoptosis and in various physiological processes. PMID: 12970870
metallothionein measured in renal specimens from cadaver kidneys was restricted to tubular cells with no differences between controls and patients with death due to chronic diseases PMID: 15812196
The overexpression of human MT1A gene dynamically affected cell viability, and the effect was influenced by zinc and cadmium ions. PMID: 16087360
MT-II mRNA expression may be involved in cell proliferation in the livers of patients with chronic HCV infection. PMID: 16107899
+647 MT1a genetic polymorphism may be essential for longevity in women. PMID: 16955215
analysis of glial fibrillary acidic protein, metallothionein, and MHC II expression in human, rat and mouse cells PMID: 17008879
The findings define a pathway for cellular metal acquisition. The results suggest a function of MT in intercellular communication. PMID: 17111383
One biomarker which has recently shown to be expressed in various human tumors but still less reported in carcinoma is metallothionein. PMID: 17373731
The partially metallated and metal-free metallothionein-1a species are stable intermediates and thus may have a potential role in the currently undefined function of metallothionein. PMID: 17388808
The goals of this study were to define the expression of the isoforms of MT 1, 2, 3 at both mRNA and protein levels, in normal prostate, benign prostatic hyperplasia (BPH) and malignant PC-3 cells. PMID: 18208603
the association of the +647 A/C MT1A polymorphism with diabetes mellitus 2 and cardiovascular complications PMID: 18249147
the interleukin-6 and metallothionein 1a genes act in a concerted manner to control zinc-regulated gene expression PMID: 18316168
Metal exchange in metallothioneins: a novel structurally significant Cd(5) species in the alpha domain of MT1A. PMID: 18429853
This study provides the necessary data establishing unambiguously the noncooperative nature of cadmium binding to both isolated domains and the combined beta-domains (beta-rhMT) of human MT-1a. PMID: 18533113
Lupus nephritis is associated with significant alterations in renal MT-I+II expression. Important prognostic information can be deduced from the renal MT-I+II expression profile in systemic lupus erythematosus patients with nephritis. PMID: 18601746
MT-IA mRNA expression in HPBLs may be used as a biomarker for renal dysfunction in occupational cadmium exposure. PMID: 19359654
HIF-1alpha expression qualified as an independent prognostic and characterised an aggressive cancer phenotype associated with an increased expression of MT. PMID: 19529947

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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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