Recombinant Human Cystine/Glutamate Transporter (SLC7A11) Protein (His)

Name: Recombinant Human Cystine/Glutamate Transporter (SLC7A11) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07630P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Cystine/Glutamate Transporter (SLC7A11) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9UPY5
Target Symbol	SLC7A11
Synonyms	(Amino acid transport system xc-)(Calcium channel blocker resistance protein CCBR1)(Solute carrier family 7 member 11)(xCT)
Species	Homo sapiens (Human)
Expression System	in vitro E.coli expression system
Tag	N-10His
Target Protein Sequence	MVRKPVVSTISKGGYLQGNVNGRLPSLGNKEPPGQEKVQLKRKVTLLRGVSIIIGTIIGAGIFISPKGVLQNTGSVGMSLTIWTVCGVLSLFGALSYAELGTTIKKSGGHYTYILEVFGPLPAFVRVWVELLIIRPAATAVISLAFGRYILEPFFIQCEIPELAIKLITAVGITVVMVLNSMSVSWSARIQIFLTFCKLTAILIIIVPGVMQLIKGQTQNFKDAFSGRDSSITRLPLAFYYGMYAYAGWFYLNFVTEEVENPEKTIPLAICISMAIVTIGYVLTNVAYFTTINAEELLLSNAVAVTFSERLLGNFSLAVPIFVALSCFGSMNGGVFAVSRLFYVASREGHLPEILSMIHVRKHTPLPAVIVLHPLTMIMLFSGDLDSLLNFLSFARWLFIGLAVAGLIYLRYKCPDMHRPFKVPLFIPALFSFTCLFMVALSLYSDPFSTGIGFVITLTGVPAYYLFIIWDKKPRWFRIMSEKITRTLQIILEVVPEEDKL
Expression Range	1-501aa
Protein Length	Full Length
Mol. Weight	58.2 kDa
Research Area	Cell Biology
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	Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate.
Subcellular Location	Membrane; Multi-pass membrane protein.
Protein Families	Amino acid-polyamine-organocation (APC) superfamily, L-type amino acid transporter (LAT) (TC 2.A.3.8) family
Database References	HGNC: 11059 OMIM: 607933 KEGG: hsa:23657 STRING: 9606.ENSP00000280612 UniGene: PMID: 28630426 In some breast cancer cells, xCT antiporter expression is upregulated through the antioxidant transcription factor Nrf2 and contributes to their requirement for glucose as a carbon source. PMID: 28429737 accumulated mutant-p53 protein suppresses the expression of SLC7A11, a component of the cystine/glutamate antiporter, system xC(-), through binding to the master antioxidant transcription factor NRF2. PMID: 28348409 System xC(-)-mediated TrkA activation therefore presents a promising target for therapeutic intervention in cancer pain treatment. PMID: 29761734 High expression of cystine-glutamate antiporter SLC7A11 is associated with advanced pathological stages of liver carcinoma. SLC7A11 overexpression is a novel biomarker and a potential unfavorable prognostic factor as well as a potential therapeutic target for liver carcinoma. PMID: 29528250 the level of antisense SLC7A11 was markedly reduced in epithelial ovarian cancer tissues and cell lines compared with those of normal control; reduction of antisense SLC7A11 level prompted ovarian cancer cell migration mainly by suppressing the expression of SLC7A11 PMID: 29441937 CD44v9 in tumor specimens has potential as a novel indicator for identifying a cisplatin-chemoresistant population among urothelial cancer patients. CD44v8-10 contributes to reactive oxygen species defenses, which are involved in chemoresistance, by promoting the function of xCT, which adjusts the synthesis of glutathione. PMID: 29385995 Oncogenic PIK3CA alters methionine and cysteine utilization, partly by inhibiting xCT to contribute to the methionine dependency phenotype in human breast cancer cells. PMID: 29259101 these observations suggest that SLC7A11 may be a vital biomarker for the diagnosis and prognosis in human laryngeal squamous cell carcinoma (LSCC) and targeting SLC7A11 appears to be a potentially significant method for LSCC treatment. PMID: 29048627 Aberrant neuronal or neuroendocrine system may be involved in the suppressed reproductive performance in xCT deficient male mice. PMID: 28974116 overexpression of SLC7A11 in the context of glioblastoma multiforme may contribute to tumor progression. PMID: 28610554 miR-375 served as a tumor suppressor via regulating SLC7A11. PMID: 28627030 As targets of oncogenes with intrinsic tyrosine kinase activity, STAT3 and STAT5 become constitutively active in hematologic neoplasms and solid tumors, promoting cell proliferation and survival and modulating redox homeostasis via regulation xCT expression. (Review) PMID: 28202313 Authors found that the xCT expression was increased in peripheral blood monocyte of active tuberculosis. xCT expression in macrophage was induced by Mycobacterium tuberculosis (Mtb) through TLR2/Akt- and p38-dependent signaling pathway. PMID: 27129162 Genetic and pharmacological inhibition of xCT potentiated the cytotoxic effects of aspirin plus sorafenib; this effect was diminished by xCT overexpression. Low-dose aspirin plus sorafenib enhanced the cytotoxicity of cisplatin in resistant HNC cells through xCT inhibition and oxidant and DNA damage. PMID: 28057599 MUC1-C binds directly with CD44v and in turn promotes stability of xCT in the cell membrane PMID: 26930718 simultaneous mutations at all four acetylation sites completely abolish its ability to regulate metabolic targets, such as TIGAR and SLC7A11. Moreover, p53(4KR) is still capable of inducing the p53-Mdm2 feedback loop, but p53-dependent ferroptotic responses are markedly abrogated PMID: 27705786 ARF inhibits tumor growth by suppressing the ability of NRF2 to transcriptionally activate its target genes, including SLC7A11, a component of the cystine/glutamate antiporter that regulates reactive oxygen species (ROS)-induced ferroptosis. PMID: 28985506 Mechanistically, CD44v interacts with and stabilizes xCT and thereby promotes the uptake of cysteine for glutathione synthesis and stimulates side-population cell enrichment. PMID: 27279909 ATF4 expression fosters the malignancy of primary brain tumors and increases proliferation and tumor angiogenesis; experiments revealed that ATF4-dependent tumor promoting effects are mediated by transcriptional targeting the glutamate antiporter xCT PMID: 28553953 Identify mTORC2 as a critical regulator of amino acid metabolism in cancer via phosphorylation of the cystine-glutamate antiporter xCT. mTORC2 phosphorylates serine 26 at the cytosolic N terminus of xCT, inhibiting its activity. PMID: 28648777 Data suggest that glucose starvation of various neoplasm cell lines induces SLC7A11 expression; SLC7A11 overexpression decreases intracellular glutamate, an alternative source of metabolic energy; provision of alpha-ketoglutarate, a key downstream metabolite of glutamate, restores survival in SLC7A11-overexpressing neoplasm cell lines under glucose starvation. PMID: 28630042 Results suggest that expression of SLC7A11 in the context of glioma contributes to tumorigenesis, tumor progression, and resistance to standard chemotherapy. PMID: 27658422 High SLC7A11 expression is associated with glioma. PMID: 26980765 The most frequent SLC7A7 mutation in Japanese LPI patients is p.R410*, which is a founder effect mutation in northern Japan. PMID: 26865117 While the transsulfuration pathway plays a primary role in supplying Cys to the redox system in the liver, xCT is induced in cases of emergencies, by compensating for Cys supply systems. PMID: 28081640 Although LCN2 increased intracellular iron concentrations, LCN2-induced GSH may catalyze and override oxidative stress via CD44 and xCT, and subsequently enhance the survival of clear cell carcinoma tumor cells in oxidative stress-rich environment. PMID: 26729415 Study demonstrated that the mRNA expression levels of the two system xc- subunits, SLC7A11 and SLC3A2, in peripheral white blood cells are lowered in patients with schizophrenia than healthy individuals PMID: 26540405 the rate of cystine uptake was significantly faster than the rate of glutamate release in human glioma cells. PMID: 26252954 increased SLC7A11 expression predicted shorter malignant glioma patient survival. PMID: 26019222 We discovered that many genes involved in oxidative stress/antioxidant defense system, apoptosis/anti-apoptosis/cell death, and cellular response to unfolded proteins/topologically incorrect proteins are potentially regulated by xCT. PMID: 25860939 Data indicate that cystine-glutamate exchange transporter protein SLC7A11 mRNA is regulated by cellular stress and nonsense-mediated RNA decay (NMD). PMID: 25399695 Sulfasalazine, a relatively non-toxic drug that targets cystine transporter, may, in combination with CDDP, be an effective therapy for colorectal cancer. PMID: 26254540 These observations suggest that the expression of xCT in esophageal squamous cell carcinoma (ESCC) cells might affect the G1/S checkpoint and impact on the prognosis of ESCC patients PMID: 23771433 Our findings indicate that miRNA-27a negatively regulates SLC7A11 in cisplatin-resistant bladder cancer, and shows promise as a marker for patients likely to benefit from cisplatin-based chemotherapy PMID: 24516043 Results show that Nrf2 and ATF4 were upregulated by proteasome inhibition and cooperatively enhance human xCT gene expression upon proteasome inhibition. PMID: 25002527 IGF-I regulates cystine uptake and cellular redox status by activating the expression and function of xCT in estrogen receptor-positive (ER(+)) breast cancer cells by a mechanism that relies on the IGF receptor substrate-1 (IRS-1). PMID: 24686172 the xCT antiporter, which is expressed on one-third of triple-negative breast tumors in this study, may have a role in glutamine updake and dependence PMID: 24094812 These findings suggest that xCT is an independent predictive factor in glioblastomas PMID: 23096413 The pathways modify system activity beyond the level of xCT transcription, including regulation on the level of membrane trafficking and substrate availability, especially the regulation by glutamate transport through excitatory amino acid transporters. PMID: 21369940 Both IGF-1 and TGF-beta stimulated system xc-mediated cystine uptake in dental pulp cells. PMID: 21689549 Results reveal that increased expression of the cystine/glutamate antiporter system xCT in multiple sclerosis provides a link between inflammation and excitotoxicity in demyelinating diseases. PMID: 21639880 SLC7A11 is a functional target gene of the BACH1 transcription factor according to ChIP-seq and knockdown analysis in HEK 293 cells. PMID: 21555518 Data show that SLC7A11 is the direct target of miR-26b and its expression is remarkably increased in both breast cancer cell lines and clinical samples. PMID: 21510944 Review discusses system xc- function in vitro and in vivo, its role as an ambivalent drug target, and the relevance of oxytosis mediated by inhibition of xCT for identification of neuroprotective proteins and signaling pathways. PMID: 20053169 The cystine/glutamate antiporter demonstrates its major role of cystine and glutamate transport while modulating intracellular glutathione content and efflux in dendritic cells during cell differentiation and cross-presentation in a transgenic system. PMID: 20733204 x(c)(-) transporter provides a useful target for glioma therapy. PMID: 20007406 Cys(327) is a functionally important residue accessible to the aqueous extracellular environment and is structurally linked to the permeation pathway and/or the substrate binding site PMID: 14722095 topological model for xCT of 12 transmembrane domains with the N and C termini located inside the cell PMID: 15151999 Expression of Tat led to decrease in glutathione and increase in gamma-glutamyl transpeptidase. The transport function of xc-was upregulated and was accompanied by increases in mRNAs for xCT and 4F2hc and in corresponding protein levels. PMID: 15326101

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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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