Recombinant Human Iron-Sulfur Cluster Assembly Enzyme Iscu, Mitochondrial (ISCU) Protein (GST)

Name: Recombinant Human Iron-Sulfur Cluster Assembly Enzyme Iscu, Mitochondrial (ISCU) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08665P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Iron-Sulfur Cluster Assembly Enzyme Iscu, Mitochondrial (ISCU) 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	Q9H1K1
Target Symbol	ISCU
Synonyms	2310020H20Rik; HML; hnifU; Iron sulfur cluster assembly enzyme ISCU mitochondrial; Iron sulfur cluster scaffold homolog (E. coli); Iron sulfur cluster scaffold homolog; Iron-sulfur cluster assembly enzyme ISCU; Iscu; IscU iron sulfur cluster scaffold homolog; ISCU_HUMAN; ISU2; MGC74517; mitochondrial; NIFU; NifU like N terminal domain containing; NifU like N terminal domain containing protein; NifU like protein; NifU-like N-terminal domain-containing protein; NifU-like protein; NIFUN; Nitrogen fixation cluster like; OTTHUMP00000238760; OTTHUMP00000238761; OTTHUMP00000238762; OTTHUMP00000238764; OTTHUMP00000238765
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQEPKKGEAEKK
Expression Range	1-167aa
Protein Length	Full Length
Mol. Weight	45.0kDa
Research Area	Signal Transduction
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	Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic Functions as a cytoplasmic scaffold protein for the de novo synthesis of iron-sulfur clusters in the cytoplasm.
Subcellular Location	[Isoform 1]: Mitochondrion.; [Isoform 2]: Cytoplasm. Nucleus.
Protein Families	NifU family
Database References	HGNC: 29882 OMIM: 255125 KEGG: hsa:23479 STRING: 9606.ENSP00000310623 UniGene: PMID: 30031876 we report the first heterozygous dominant mutation in ISCU; notably, this alteration resulted in a similar phenotype as the recessive ISCU disease previously described. PMID: 29079705 When ISCU was replaced by the fully structured variant ISCU(M108I), the addition of rdFDX2 to the [NIA-ISCU(M108I)-FXN]2 complex led to the release of FXN. Thus, the displacement of FXN by rdFDX2 explains the failure of FXN to stimulate Fe-S cluster assembly on ISCU(M108I). PMID: 29406711 We have shown that ASO treatment diminished aberrant splicing and increased ISCU protein levels in both patient fibroblasts and patient myotubes in a concentration dependent fashion. Upon ASO treatment, levels of SDHB in patient myotubular cell lines increased to levels observed in control myotubular cell lines PMID: 28007899 The NFS1/ISD11 complex further interacts with scaffold protein ISCU and regulator protein frataxin, thereby forming a quaternary complex for Fe-S cluster formation. PMID: 28271877 Molecular dynamics flexible fitting of protein structures docked into the EM map of the model revealed a [FXN(42-210)]24.[NFS1]24.[ISD11]24.[ISCU]24 complex, consistent with the measured 1:1:1:1 stoichiometry of its four components. PMID: 27519411 ISCU expression was decreased in the majority of human liver cancer tissues, and its reduced expression was significantly associated with p53 mutation. PMID: 26560363 Thus, driven by acquired (hypoxia) or genetic causes, the miR-210-ISCU1/2 regulatory axis is a pathogenic lynchpin causing iron-sulfur deficiency and pulmonary hypertension. PMID: 25825391 The core Fe-S biosynthetic enzymatic complex generated [2Fe-2S] cluster intermediates that converted to stable [2Fe-2S] clusters bound to uncomplexed ISCU2. PMID: 26016389 IscU is a new substrate of MK2 both in Drosophila cells and in human cells PMID: 25204651 Fe-S assembly protein (ISCU2) and frataxin convert substrates l-cysteine, ferrous iron, and electrons into Fe-S clusters. PMID: 24971490 the G50E iron-sulfur cluster scaffold protein (ISCU) mutation has a role in mitochondrial myopathy PMID: 24573684 NFS1 binds preferentially to the D-state of ISCU while mtHSP70 binds preferentially to the D-state of ISCU and HSC20 binds preferentially to the S-state of ISCU. PMID: 23940031 mTORC1 associates with ISCU and phosphorylates ISCU at serine 14. This phosphorylation stabilized ISCU protein. PMID: 23508953 MicroRNA-210 correlates negatively with its gene target ISCU at the protein and mRNA level. MicroRNA-210 correlated with positive outcome variables PMID: 23449350 ISCU protein deficiency in patients results from muscle-specific mis-splicing and oxidative stress. PMID: 23035118 this study unveiled a signaling axis of HIF-1alpha/miRNA-210/iron-sulfur cluster scaffold protein in a subset of head and neck paragangliomas that could have an impact on SDHB protein stability by a mechanism independent of succinate dehydrogenase mutations PMID: 22977270 Photoreactive heterotrifunctional chemical cross-linking confirmed the interaction between frataxin and ISCU in the presence of iron and validated that transient interactions can be covalently trapped with this method. PMID: 22897349 iron-sulfur cluster scaffold homologue down-regulation by miR-210 perturbing trophoblast iron metabolism is associated with defective placentation PMID: 21801864 Exchange of [2Fe-2S] centers between glutaredoxin 2 and the cluster scaffold protein ISU, supports a direct link for glutaredoxin 2 and glutathione involvement in ISU promoted Fe-S cluster biosynthesis. PMID: 21437321 Data show that the highest level of incorrectly spliced ISCU mRNA was found in skeletal muscle. PMID: 21165651 miR-210 mediates a new mechanism of adaptation to hypoxia, by regulating mitochondrial function via iron-sulfur cluster metabolism and free radical generation PMID: 20436681 ISCU and COX10 are target genes of miR-210 related to mitochondrial metabolism PMID: 20498629 Data suggest that frataxin may be involved in the biosynthesis of iron-sulphur proteins such as IscU1 not only within the mitochondria, but also in the extramitochondrial compartment. PMID: 16091420 Functional analysis of the mitochondrial and cytosolic isoforms of the human Fe-S cluster scaffold protein, ISCU. PMID: 16517407 the cytosolic form of ISCS is a functional cysteine desulfurase that can collaborate with cytosolic ISCU to promote de novo iron-sulfur cluster formation PMID: 16527810 Intron mutation in the ISCU gene, leading to incorrectly spliced mRNA, is the cause of myopathy with lactic acidosis in this family. PMID: 18296749 Gene ISCU was identified as a candidate within a region of shared homozygosity among patients with myopathy with severe exercise intolerance and myoglobinuria. PMID: 18304497 the iron-dependent binding affinity of each frataxin derivative to the iron-sulfur cluster scaffold protein ISU is found to be similar to that of native frataxin PMID: 18425540 a new ISCU mutation in iron-sulphur cluster deficiency myopathy PMID: 19567699 Results identify the iron-sulfur cluster assembly proteins (ISCU1/2) as direct targets for repression by the hypoxia-induced microRNA-210. PMID: 19808020

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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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