Recombinant Human High Affinity Copper Uptake Protein 1 (SLC31A1) Protein (His-SUMO), Active

Beta LifeScience SKU/CAT #: BLC-05647P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Activity Measured by its binding ability in a functional ELISA. Immobilized SLC31A1 at 5 μg/ml can bind human LGALS8, the EC 50 of human LGALS8 is 373.90-524.30 μg/ml.
Activity Measured by its binding ability in a functional ELISA. Immobilized SLC31A1 at 5 μg/ml can bind human LGALS8, the EC 50 of human LGALS8 is 373.90-524.30 μg/ml.
Greater than 90% as determined by SDS-PAGE.
Activity Measured by its binding ability in a functional ELISA. Immobilized SLC31A1 at 5 μg/ml can bind human LGALS8, the EC 50 of human LGALS8 is 373.90-524.30 μg/ml.

Recombinant Human High Affinity Copper Uptake Protein 1 (SLC31A1) Protein (His-SUMO), Active

Beta LifeScience SKU/CAT #: BLC-05647P
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Product Overview

Description Recombinant Human High Affinity Copper Uptake Protein 1 (SLC31A1) Protein (His-SUMO), Active is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Activity Measured by its binding ability in a functional ELISA. Immobilized SLC31A1 at 5 μg/ml can bind human LGALS8, the EC50 of human LGALS8 is 373.90-524.30 μg/ml.
Uniprotkb O15431
Target Symbol SLC31A1
Synonyms SLC31A1; COPT1; CTR1; High affinity copper uptake protein 1; Copper transporter 1; hCTR1; Solute carrier family 31 member 1
Species Homo sapiens (Human)
Expression System in vitro E.coli expression system
Tag N-6His-SUMO
Target Protein Sequence MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFGFKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH
Expression Range 1-190aa
Protein Length Full Length
Mol. Weight 37.1kDa
Research Area Others
Form Lyophilized powder
Buffer Lyophilized from 20 mM Tris-HCl, 0.15 M NaCl, 0.05% DDM, 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 High-affinity, saturable copper transporter involved in dietary copper uptake.
Subcellular Location Cell membrane; Multi-pass membrane protein.
Protein Families Copper transporter (Ctr) (TC 1.A.56) family, SLC31A subfamily
Database References

Gene Functions References

  1. combination of desferal with oxaliplatin can overcome cervical cancer oxaliplatin resistance through the regulation of hCtr1 and TfR1 PMID: 27384479
  2. Study showed that NEAT1 could function as a competing endogenous lncRNA in lung cancer, mediating CTR1 by sponging hsa-mir-98-5p. PMID: 27270317
  3. This result indicates that the formation of copper-finger protein of Sp1 is the molecular basis of copper sensing for the transcriptional regulation of hCtr1 in mammalian cells. PMID: 28759062
  4. we assessed the role of miR-21 in mediating renal cell carcinoma chemoresistance and further showed that miR-21 silencing significantly (1) increased chemosensitivity of paclitaxel, 5-fluorouracil, oxaliplatin, and dovitinib; (2) decreased expression of multi-drug resistance genes; and (4) increased SLC22A1/OCT1, SLC22A2/OCT2, and SLC31A1/CTR1 platinum influx transporter expression PMID: 28714373
  5. Gene duplication and neo-functionalization in the evolutionary and functional divergence of the metazoan copper transporters Ctr1 and Ctr2 PMID: 28507097
  6. It has been demonstrated in ovarian cancer cells that cisplatin resistance and uptake correlates with reduced CTR1 and LRRC8A protein expression/activity and a concomitant upregulation in cisplatin exporting transporters (ATP7A, ATP7B), which implies that the resistant cells have a reduced ability to accumulate cisplatin and activate proapoptotic transporters for osmolytes. PMID: 27112899
  7. CTR1 recycling via clathrin-mediated and Rab11 pathways enable cells to dynamically modulate copper entry PMID: 26945057
  8. C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1 PMID: 26745413
  9. Studied the interaction of CTR1 and CTR2 in fully malignant HEK293T and OVCAR8 human ovarian cancer cells using a CRISPR-Cas9 knock out system. PMID: 26205368
  10. High CTR1 Expression is associated with poor response to chemotherapy in Muscle-invasive Bladder Cancer. PMID: 26851002
  11. Gene silencing of either CTR1 or DMT1 did not affect copper accumulation in cells, but deficiency in both CTR1 and DMT1 resulted in a complete inhibition of copper uptake. PMID: 26067577
  12. Two methionine residues in the MXXXM motif of of the CTR1 second transmembrane domain are important for binding to silver. PMID: 26061257
  13. CTR1, ATP7A, and lysyl oxidase were upregulated in the lung tissues and pulmonary arteries of mice with hypoxia-induced pulmonary hypertension and pulmonary arterial smooth muscle cells. PMID: 24614111
  14. Data suggest that SLC31A1 and SLC31A2, despite being structurally closely related and sharing important amino acid motifs, play different roles in copper homeostasis and in platinum-based chemotherapy of neoplasms. [REVIEW] PMID: 24703712
  15. allele distribution of the SLC31A1 was not different between group N and O, and out of the 11 SNPs of the SLC22A2 gene only the allele distribution of the nonsynonymous SNP was significantly different between patients who experienced ototoxicity PMID: 25823781
  16. Extracellular copper concentrations regulate the levels of CTR1 through internalisation and degradation, the addition of prolactin, inhibits the degradation of CTR1, thus promoting copper uptake by mammary epithelial cells. PMID: 24485600
  17. NSC73306 is a transport substrate of CTR1 PMID: 24800945
  18. The data collected here shows that the Atox1 keeps its dimer nature also in the presence of the CTR1 c-terminal domain; however, two geometrical states are assumed by the Atox1. PMID: 24837030
  19. CTR1 expression may be necessary for therapeutic efficacy of platinum based drugs in non-small cell lung cancer treatment. PMID: 24792335
  20. Cisplatin transcriptionally induces the expression of human Ctr1 in time- and concentration-dependent manners. PMID: 24132751
  21. Knockdown of CTR1 expression in human umbilical cord endothelial cells increases cell proliferation and migration. PMID: 24039729
  22. Duodenal CTR1 mRNA and protein expression was decreased in Wilson's disease patients, while ATP7A mRNA and protein production was increased. This can be a defense mechanism against systemic copper overload resulting from functional impairment of ATP7B. PMID: 23963605
  23. This study demonistrated that Inhibition of human high-affinity copper importer Ctr1 orthologous in the nervous system of Drosophila ameliorates Abeta42-induced Alzheimer's disease-like symptoms. PMID: 23827522
  24. The patients with tumors showing high expression levels of at least one of OATP1B3 and CTR1 had potentially longer disease-free survival. PMID: 23782748
  25. Results show that hCTR1 elements on the intracellular side of the hCTR1 pore, including the carboxyl tail, are not essential for permeation, but serve to regulate the rate of copper entry. PMID: 23658018
  26. Depletion of glutathione decreases cellular copper uptake mediated by human copper transporter 1. PMID: 23426973
  27. Our findings imply that reduced CTR1 expression accounts for decreased cisplatin accumulation and represents one of the determinants of cisplatin resistance in A2780cis cell line PMID: 23010323
  28. Cisplatin induces drug resistant phenotype by decreasing the protein level of CTR1 in human esophageal squamous carcinoma cell line EC109. PMID: 21602128
  29. genetic association study in Han population in China: Data suggest that SNPs in SLC31A1 (rs7851395; rs12686377) are associated with resistance to platinum compounds as antineoplastics and survival outcomes in non-small cell lung carcinoma patients. PMID: 22725681
  30. This review explains how modulating cellular copper availability could influence treatment efficacy in platinum-based cancer chemotherapy through hCtr1 regulation[review] PMID: 22962276
  31. CTR1 plays an essential role in cisplatin toxicity and could be considered as a predictor for pretreatment evaluation in lung cancer patients. PMID: 22516052
  32. The cells expressing the hCTR1 mutants of histidine-rich motifs in the N-terminus (H22-24A, NHA) resulted in a higher basal copper level in the steady state compared to those expressing wild-type protein. PMID: 22552365
  33. There was little difference in rates/kinetics of uptake of copper in the Ctr1+/+ and -/- cells. Endocytosis was not involved. PMID: 22354499
  34. Structure of CTR1 confirms that two triads of methionine residues delineate the intramembranous region of the transporter, and further identifies two additional methionine triads that are located in the extracellular N-terminal part of the transporter. PMID: 22569840
  35. basal expression of Ctr1 is regulated by HIF2alpha; however, the induction by hypoxia is a HIF2alpha-independent event PMID: 22684009
  36. Data show that both shRNA-DMT1 and shRNA-hCTR1 cells had lower apical Fe uptake, Cu uptake, and Zn content compared to control cells. PMID: 22068728
  37. Compared the binding interactions between cisplatin, carboplatin and oxaliplatin with synthetic peptides corresponding to hCtr1 Mets motifs. PMID: 21072377
  38. Data show apical localization of Ctr1 in intestinal epithelia and suggest that increased Ctr1 apical localization in response to dietary copper limitation may represent an adaptive response to modulate Ctr1 availability at the site of copper absorption. PMID: 20699218
  39. Ctr1 is an important transport protein in the accumulation of silver in mammalian cells. PMID: 20569931
  40. Identified as dominant hinge regions, CTR1's MxxxM and GxxxG motifs were shown to have significant roles in functional movements characterized by the two slowest modes of motion. PMID: 20534491
  41. findings reveal a high level of conservation between the mammalian and insect Ctr1-type copper importers PMID: 19856191
  42. Results demonstrate that co-exposure of tumor cells to emodin or DRB with cisplatin inhibits platinum drug uptake by impacting the hCtr1 transporter. PMID: 19529937
  43. Sequence analysis demonstrated SLC31A1 on chromosome 9 was rearranged with breaks occurring within its intron. SLC31A1 lies close to BSPRY which is a candidate for cleft lip/palate involvement. PMID: 19929093
  44. fundamentally conserved mechanism for high affinity copper uptake through the Ctr proteins in yeast and humans PMID: 11983704
  45. biochemical characterization and subcellular localization PMID: 12023893
  46. observations demonstrate that, although Ctr1 is critical for both cellular copper uptake and embryonic development, mammals possess additional biochemically distinct functional copper transport activities PMID: 12177073
  47. Results suggest that human copper transporter 1 (CTR1) spans the membrane at least six times, permitting formation of a channel, which is consistent with its proposed role as a copper transporter. PMID: 12466020
  48. hCtr1-mediated copper uptake into mammalian cells is regulated by a post-translational mechanism involving copper-stimulated endocytosis and degradation of the transporter PMID: 12501239
  49. there are common biochemical mechanisms regulate both transport and trafficking functions of hCtr1 PMID: 14976198
  50. there is a direct interaction between cisplatin and the hCtr1 protein; cisplatin and copper have distinct biochemical consequences on this transporter PMID: 15326162

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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