Recombinant Human Superoxide Dismutase [Cu-Zn] (SOD1) Protein (His), Active

Name: Recombinant Human Superoxide Dismutase [Cu-Zn] (SOD1) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05559P
Availability: InStock

Collections: All products, Featured enzyme molecules, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Superoxide Dismutase [Cu-Zn] (SOD1) Protein (His), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The potency per mg was determined by pyrogallol autoxidation method and was found to be more than 1600 U/mg.
Uniprotkb	P00441
Target Symbol	SOD1
Synonyms	ALS; ALS1; Amyotrophic lateral sclerosis 1 adult; Cu/Zn SOD; Cu/Zn superoxide dismutase; Epididymis secretory protein Li 44; HEL S 44; Homodimer; hSod1; Indophenoloxidase A; IPOA; Mn superoxide dismutase; SOD; SOD soluble; SOD1; SOD2; SODC; SODC_HUMAN; Superoxide dismutase [Cu-Zn]; Superoxide dismutase 1; Superoxide dismutase 1 soluble; Superoxide dismutase Cu Zn; Superoxide dismutase cystolic
Species	Homo sapiens (Human)
Expression System	E.Coli
Tag	N-10His
Complete Sequence	MGHHHHHHHH HHSSGHIEGR HMTYARAAAR QARALE+ATKA VCVLKGDGPV QGIINFEQKE SNGPVKVWGS IKGLTEGLHG FHVHEFGDNT AGCTSAGPHF NPLSRKHGGP KDEERHVGDL GNVTADKDGV ADVSIEDSVI SLSGDHCIIG RTLVVHEKAD DLGKGGNEES TKTGNAGSRL ACGVIGIAQ
Expression Range	2-154aa
Protein Length	Full Length of Mature Protein
Mol. Weight	20 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	0.2 μm filtered PBS, pH 7.4, lyophilized
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.

Target Details

Target Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular Location	Cytoplasm. Mitochondrion. Nucleus.
Protein Families	Cu-Zn superoxide dismutase family
Database References	HGNC: 11179 OMIM: 105400 KEGG: hsa:6647 STRING: 9606.ENSP00000270142 UniGene: PMID: 30142602 Study results in transgenic mice carrying human SOD1 gene and analysis of cerebrospinal fluid as well as the spinal cord homogenate amyotrophic lateral sclerosis (ALS) patients suggest that metal-deficiency in mutant SOD1 at its copper-binding site is one of the earliest pathological features in SOD1-ALS. PMID: 29551730 A stable core of the SOD2 that unfolds last and refolds first, and directly observe several distinct misfolded states that branch off from the native folding pathways at specific points after the formation of the stable core. PMID: 29192167 The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis. PMID: 28711596 the introduction of SOD1(G93A) and TDP43(A315T), established Amyotrophic lateral sclerosis (ALS)-related mutations, changed the subcellular expression and localization of RNAs within the neurons, showing a spatial specificity to either the soma or the axon. Altogether, we provide here the first combined inclusive profile of mRNA and miRNA expression in two ALS models at the subcellular level. PMID: 28300211 Shorter activated partial thromboplastin time and increased SOD levels might be useful hemostatic markers in patients with type 2 diabetes mellitus. PMID: 30143488 In this study we demonstrate dynamic changes in the number of calretinin- (CR) and neuropeptide Y-expressing (NPY) interneurons in the motor cortex of the familial hSOD1(G93A) ALS mouse model, suggesting their potential involvement in motor neuron circuitry defects PMID: 28294153 Our results suggest that SOD1 mutation is the most common cause of amyotrophic lateral sclerosis(ALS) in Chinese populations and that the mutation spectrum of ALS varies among different ethnic populations PMID: 28291249 Weak significance was observed for a protective effect of the TT genotype of rs1041740 in the SOD1 gene relative to Type 1 Diabetes development (OR 0.318, 95% CI 0.092-0.959, p = 0.056). PMID: 29924645 SOD1 is S-acetylated in spinal cord homogenates from ALS and non-ALS subjects. The degree of S-acylation is highest for SOD1-CCS heterodimers and lowest for SOD1 monomers. PMID: 28120938 Study suggests that endoplasmic reticulum stress increases the susceptibility of SOD1WT to aggregate during aging, operating as a possible risk factor for developing amyotrophic lateral sclerosis. PMID: 30038021 Metallation and oxidation of SOD1 stabilize the native, mature conformation and decrease the number of detected excited conformational states. PMID: 29483249 results thus shed light on the role of local unfolding and conformational dynamics in aggregation of SOD1 PMID: 29369331 Certain SOD1 mutants, viz. His80Arg and Asp83Gly, were recognized that were more damaging to the Zn binding loop than all other mutants, leading to a loss of Zn binding with altered coordination of the Zn ion. Furthermore, the conformational stability, compactness, and secondary structural alteration of the His80Arg and Asp83Gly mutants were monitored using distinct parameters. PMID: 28271284 describe here two cases of apparently sporadic amyotrophic lateral sclerosis associated with mutations, respectively, in SOD1 and TARDP genes PMID: 27494151 that global changes in DNA methylation might contribute to the ALS phenotype in carriers of not fully penetrant SOD1 mutations PMID: 28859526 The present study indicating that although the Ins/Del polymorphism of SOD1 is associated with the SOD1 expression levels, this polymorphism is not associated with the risk of dependency to heroin. PMID: 29165112 The mutant human SOD1-G93A protein induced axonal and myelin degeneration during the progression of Amyotrophic Lateral Sclerosis in a mouse model and participated in axon remyelination and regeneration in response to injury. PMID: 29742495 SOD1 oligomer and not the mature form of aggregated fibril is critical for the neurotoxic effects in the model of amyotrophic lateral sclerosis. PMID: 29666246 Data suggest that serum SOD1 levels are decreased in patients with controlled or uncontrolled acromegaly as compared to healthy subjects; in acromegaly, SOD1 levels are not associated with MnSOD/SOD2 polymorphisms. PMID: 29046499 Ovariectomy resulted in earlier disease onset and attenuated the anti-inflammatory and anti-apoptotic actions of estrogen in hSOD1-G93A transgenic mice. PMID: 29394243 a measure of hydrogen bond stability in conformational states was studied with elastic network analysis of 35 SOD1 mutants. PMID: 29431095 The genetic mutations of SOD1 caused amyotrophic lateral sclerosis PMID: 29478603 the study provides a better understanding over the profound effect of mutation on SOD1, both structurally and functionally, using computational approaches. PMID: 28899654 SOD1 amino acid residues forming these pathogenic hydrogen bonds are found in zinc-binding and electrostatic loops as well as at zinc-binding sites and are in contact with SOD1 aggregates, which implies that these regions are sensitive to perturbations from pathogenic mutations. PMID: 28950184 show a clear variation of the different SOD1 mutants to associate with mitochondrial-enriched fractions with a correlation between mutation severity and this association PMID: 28715630 Study shows that in senile cataracts, SOD1 expression decreased significantly. Both H3 and H4 were deacetylated at -600 bp of the SOD1 promoter of cataract lenses, and hypoacetylated at -1500, -1200, and -900 bp. In hypoacetylated histones, the hypoacetylation pattern differed among the cataracts sub-types. Further functional data provide evidence that histone acetylation plays an essential role in the regulation of SOD1. PMID: 27703255 Study shows that SOD1 forms fibrillar aggregates under quiescent conditions at near-physiological pH, ionic strength, and temperature over a time frame of weeks; and that intermolecular disulfide bonds are not required for the protein to form aggregates, even in the absence of fibril seeds. Scrambling of intramolecular disulfide bonds is not required for aggregation. Urea denaturation increases aggregation lag time. PMID: 28585802 SOD1 G93A mutant from familial amyotrophic lateral sclerosis cases binds VDAC1 with high affinity. PMID: 27721436 Like other neurodegenerative diseases, misfolding of a specific protein is central to ALS. SOD1, the major constituent of the protein deposits in some familial and sporadic forms of ALS, propagates its misfolded conformation like prions, providing a plausible molecular basis for the focality and spreading of muscle weakness in ALS PMID: 28096265 Data show that cholecystectomy patients with enhanced levels of superoxide dismutase (SOD1) appeared to have significantly lower number of analgesic oxycodone doses during the first 24 h postoperatively (NAD24). PMID: 29848712 the structural changes and the alteration in distance between Zn and its binding residues which cause the loss of Zn binding was studied in details to delivery the foresight on the impact of the mutation in SOD1. PMID: 27555441 antioxidant activity of erythrocyte SOD is associated with dementia severity. PMID: 28965606 Results provide evidence that ALS mutant SOD1 inhibits axonal transport of mitochondria by inducing PINK1/Parkin-dependent Miro1 degradation. PMID: 28973175 Study reveals presence of glial cell proliferation in both motor (brainstem) and non-motor (hippocampus) CNS structures of hSOD1G93A ALS rats starting already at the presymptomatic stage of the disease. A specific timeline of glial response is demonstrated in the brainstem of these animals with the activation of astrocytes coming first and before disease onset, followed by activation of microglia in the symptomatic phase. PMID: 28576725 SOD1 mutations were present in 20% of familial amyotrophic lateral sclerosis (ALS) patients and 1.9% of sporadic ALS patients, while FUS mutations were responsible for 13.3% of familial ALS cases, and TARDBP mutations were rare in either familial or sporadic ALS cases. PMID: 27604643 Significant association between the SOD1 Ins/Del polymorphism and age of onset in bipolar disorder type 1. PMID: 28750571 Data provide evidence that metal binding, in addition of being necessary for SOD1 enzymatic activity, is a key factor in the aggregation process of SOD1. In particular, both demetalation and aberrant metal binding have been shown to promote misfolding and aggregation in SOD1 suggesting a possible role of metal binding in SOD1 pathological aggregation. [review] PMID: 28850080 SOD1 heterodimerization rate is influenced by mutation and is correlated with survival times in amyotrophic lateral sclerosis. PMID: 27054659 early stage influenza A virus infection induces autophagic degradation of antioxidant enzyme SOD1, thereby contributing to increased ROS generation and viral infectivity in alveolar epithelial cells. PMID: 29548827 Computational investigation of the human SOD1 mutant, Cys146Arg, that directs familial amyotrophic lateral sclerosis, has been reported. PMID: 28621357 Suggest a complex role of SOD1 in different processes leading to complications of liver cirrhosis. rs1041740 might be associated with the development of ascites and possibly plays a role in spontaneous bacterial peritonitis once ascites has developed. PMID: 28403123 SOD1 gene polymorphisms associated with susceptibility to noise-induced hearing loss. PMID: 29072670 all affected members, except the proband's father, who was unavailable for DNA analysis, showed a heterozygous mutation (c.125G>A) in exon 2 of the SOD1 gene. We found that the executive domain, attention domain, language function, calculation tasks and memory were significantly impaired in the patients with ALS compared to the healthy family members. PMID: 26069299 Slowly upper and lower motor neuron degeneration, even with non-motor clinical features, should prompt a sequencing of SOD1 PMID: 27892702 research demonstrated that erysipelas infection predisposition and its clinical characteristics are affected by age, sex and SNPs found in SOD1, SOD2, and catalase genes; presence of SOD1 G7958 alleles was linked to erysipelas' predisposition; G and A alleles of SOD1 G7958A individually were associated with lower limbs and higher body part localizations of the infection, respectively PMID: 28512644 Low SOD1 Expression Is Associated with Postoperative Pain. PMID: 29374733 Our data indicate that SOD1 is directly or indirectly involved in ALS oligodendrocyte pathology and suggest that in this cell type, some damage might be irreversible. PMID: 27688759 Gelsolin enhances the invasive capacity of colon cancer cells via elevating intracellular superoxide (O2.-) levels by interacting with Cu/ZnSOD, and gelsolin gene expression positively correlates with urokinase plasminogen activator (uPA), an important matrix-degrading protease invovled in cancer invasion. PMID: 27391159 The observation that beta-strand 5 is among the first to unfold here, but the last to unfold in simulations of loop-truncated SOD1, could imply the existence of an evolutionary compensation mechanism, which would stabilize beta-strands flanking long loops against their entropic penalty by strengthening intramolecular interactions. PMID: 28629863

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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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