Recombinant Rat Superoxide Dismutase [Cu-Zn] (SOD1) Protein (His)

Name: Recombinant Rat Superoxide Dismutase [Cu-Zn] (SOD1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00529P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Rat Superoxide Dismutase [Cu-Zn] (SOD1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07632
Target Symbol	SOD1
Species	Rattus norvegicus (Rat)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	AMKAVCVLKGDGPVQGVIHFEQKASGEPVVVSGQITGLTEGEHGFHVHQYGDNTQGCTTAGPHFNPHSKKHGGPADEERHVGDLGNVAAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Expression Range	2-154aa
Protein Length	Full Length of Mature Protein
Mol. Weight	17.3 kDa
Research Area	Cancer
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	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Cu-Zn superoxide dismutase family
Database References	KEGG: rno:24786 STRING: 10116.ENSRNOP00000002885 UniGene: Rn.6059

Gene Functions References

Results provide evidence that ALS mutant SOD1 inhibits axonal transport of mitochondria by inducing PINK1/Parkin-dependent Miro1 degradation. PMID: 28973175
SOD1 protein expression is upregulated and associated with greater oxidant production in skeletal muscle from Ts65Dn mice. PMID: 28697486
These results suggest that the superoxide anion may be the cause of the observed oxidative damage to SOD1(G93A) rat neural tissues and that the iron-sulfur clusters may be the source of poorly liganded redox active iron implicated in ALS pathogenesis. Low temperature EPR spectroscopy appears to be a valuable tool in assessing the role of metals in neurodegenerative diseases PMID: 27130034
SOD1 and zinc have roles in methotrexate-induced germ cell toxicity PMID: 28011267
A motility defect in SOD1-G93A was highly correlated with mitochondrial movement. PMID: 27464601
Diabetic testes showed decreased Nrf2, HO-1, SOD1, PCNA, and Bcl-2 expressions whereas increased COX-2, NF-kappaB, MT, IL-6, and p-ERK levels. SOD1 and GPX5 were decreased in the epididymis of diabetic rat, whereas Zn supplementation attenuated these changes. PMID: 27025721
These findings suggest that diabetes increases lipid peroxidation and decreases SOD1 levels, and treadmill exercise can mitigate diabetes-induced oxidative damage in the hippocampus. PMID: 25293488
The found of this study suggest that, from a histological standpoint, the SOD1-G93A rat is a valid model of ALS bulbar symptoms. PMID: 25825172
SOD1 has sequence homology to an antihypertensive snake bradykinin-potentiating peptide. PMID: 26047849
the knockdown of mutant SOD1 in only the motor cortex resulted in a significant delay of disease onset, expansion of lifespan, enhanced survival of spinal motor neurons,and maintenance of neuromuscular junctions PMID: 25411487
These data extend clinical findings of a more rapid disease progression in individuals with bulbar symptoms to the SOD1-G93A rat model of ALS. PMID: 24291387
Data suggest that expression of CuZnSOD/Sod1 (and mitochondrial MnSOD/Sod2) is down-regulated as retinal neurons undergo apoptosis following onset of diabetes/diabetic retinopathy. PMID: 24527463
Results highlight misfolded SOD1 as common to two Amyotrophic lateral sclerosis (ALS) rodent animal models and familial ALS patient lymphoblasts with four different SOD1 mutations. PMID: 23736301
SOD1, constitutively produced and released by microglia, is identified as an essential component of neuroprotection mediated by microglia. PMID: 22572742
both SIRT3 and PGC-1alpha protect against mitochondrial fragmentation and neuronal cell death by mutant SOD1 PMID: 22819776
Xanthine/xanthine oxidase treatment increases SOD1 and SOD2 protein and activity levels in cardiac progenitor cells. PMID: 22758933
CuZn-SOD levels were increased in the hippocampus in OLETF rats. PMID: 22981416
Data indicate that Cu-ZnSod expression decreased upon long reperfusion and trxr1 expression did not vary. PMID: 22377061
Data show that aging is associated with reduction in superoxide dismutase (SOD) Cu/Zn-SOD protein expression and total SOD enzymatic activity in mesenteric lymphatic vessel (MLV). PMID: 22540739
Cu/Zn-SOD activity was not significantly changed in response to vitamin E administration at any time points, whereas Cu/Zn-SOD mRNA levels were significantly increased after longer time points with high doses (30 and 100 mg/kg) of vitamin E. PMID: 22732938
The increased expression of antioxidant SOD1, specifically in hippocampal neurons, will provide protection from age-related cognitive decline. PMID: 21942371
dehydroepiandrosterone treatment did not alter disease progression or survival in SOD1-G93A rats PMID: 22409357
Using gastrocnemius muscles of mice overexpressing human mutant SOD1 (mutSOD1) at different disease stages. PMID: 22178654
expression of Cu,Zn-superoxide dismutase decreased significantly in the dorsal hippocampus (CA1 and CA2) and tended to decrease in ventral regions (CA3 and dentate gyrus) by the 24th hour after 3-fold exposure to hypoxia. PMID: 22451871
The present results suggested that inhibition of Shh signaling pathway exacerbated rat ischemic damage caused by pMCAO, which may be correlated with down-regulated expression of Gli1, Ptch1 and SOD1. PMID: 22133807
Data have shown that different stressors have diverse effect on hepatic CuZnSOD and MnSOD activity as well as on serum CORT level. PMID: 21625958
Thus mitochondrial dysfunction is a key early element in pathogenesis of motor neuron degeneration in transgenic SOD1 rats PMID: 21745570
rat Cu/Zn SOD can be nitrated, a modification that could lead to the depressed activity of this enzyme found in placentas from diabetic rats PMID: 20815790
Results describe changes in SOD1 immunoreactivity associated with lipid peroxidation and inflammatory responses in the hippocampi of STZ-induced type I diabetic rats. PMID: 20924670
most, but not all, properties of SOD1 remain the same with a GFP tag PMID: 20221404
Cu,Zn-superoxide dismutase increases toxicity of mutant and zinc-deficient superoxide dismutase by enhancing protein stability PMID: 20663894
Data indicate that acute and/or chronic stress models have different degrees of influence on serum corticosterone and copper-zinc/manganese superoxide dismutase subcellular protein levels. PMID: 20020182
A significant reduction of Cu,Zn-Sod-1 activity level is observed during fast speed running in the crural diaphragm muscle. PMID: 20134035
results suggest that mutant SOD1 and defective mitochondria create localized dysfunctional domains in motor axons, which may lead to progressive axonopathy in ALS PMID: 19344250
Transcriptional regulation and environmental induction of gene encoding copper- and zinc-containing superoxide dismutase. PMID: 11912919
Levels of Sod1 mRNA were significantly reduced in congestive heart failure following myocardial infarction. PMID: 14575298
Associated with copper deficiency were consistent reductions in immunoreactive SOD in erythrocytes. PMID: 15337829
Medroxyprogesterone acetate inhibits the effect of idarubicin on blood levels of this enzyme. PMID: 15372991
the role of PPARgamma is specific to events occurring during reperfusion, in which to CuZn-SOD is a mediator of neuroprotection PMID: 15618443
respiratory motor neuron loss results in significant electrophysiologic changes and diaphragmatic atrophy in SOD1 G93A rats PMID: 16084734
mutant superoxide dismutase has a role in experimental amyotrophic lateral sclerosis PMID: 16195234
Overexpression of SOD1 in whole lens prevents H2O2-induced oxidative damage (cataract formation) to the lens and subsequent control of gap junctions by protein kinase Cgamma. PMID: 16254550
Levels are not significantly altered in the rat prostate during aging and thus is unlikely to be an important factor in the evolution of epithelial cell hyperplasia. PMID: 16372329
These findings show a heterogeneous expression of Cu/Zn SOD in restricted cell types in the germinative zones and suggest a role for antioxidant Cu/Zn SOD in progenitor cells of the immature rat brain. PMID: 16567040
We hypothesized that LA might induce dissociation of p56(Lck) from CD4, thus leading to its downmodulation. PMID: 16631605
In conclusion, this study demonstrates an age-related decline in Cu/Zn-SOD and IDO activities, the two enzymes responsible for scavenging O2*-. PMID: 16688932
acute and rapid endothelial cell endocytosis of CuZn-SOD, possibly via activation of a receptor-mediated pathway PMID: 17077646
EcSOD, CuZnSOD, catalase, and MMP-2 mRNA expression did not statistically vary between aortic aneurysm and normal tissue PMID: 17196988
Ischemic attack causes a rapid response in hippocampal tissue as well as in the cerebrospinal fluid, represented by an increase in the activity of endogenous antioxidant enzymes SOD and CAT. PMID: 17215005
Data show that activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo. PMID: 17324120

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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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