Recombinant Human Ornithine Decarboxylase (ODC1) Protein (His-SUMO&Myc)

Name: Recombinant Human Ornithine Decarboxylase (ODC1) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-02896P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2) ODC1 .

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Product Overview

Description	Recombinant Human Ornithine Decarboxylase (ODC1) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P11926
Target Symbol	ODC1
Synonyms	DCOR_HUMAN; Dodc1; Odc 1; ODC; Odc1; ODC2; Ornithine decarboxylase 1; Ornithine decarboxylase 2; Ornithine decarboxylase; Ornithine decarboxylase structural 1; RNODC
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-SUMO&C-Myc
Target Protein Sequence	MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
Expression Range	1-461aa
Protein Length	Full Length
Mol. Weight	71.1 kDa
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	Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Protein Families	Orn/Lys/Arg decarboxylase class-II family
Database References	HGNC: 8109 OMIM: 165640 KEGG: hsa:4953 STRING: 9606.ENSP00000234111 UniGene: Hs.467701

Gene Functions References

Extracellular polyamines induced proliferation and cancer cell migration by inducing ODC and SSAT expression, and the Akt1-mediated pathway. PMID: 28157137
Ornithine decarboxylase (ODC) plays a key role in prostate tumorigenesis and that the polyamine pathway is altered as early as high-grade prostate intraepithelial neoplasia (HGPIN). PMID: 27770613
Findings suggest that targeting ornithine decarboxylase 1 (ODC1) could be an attractive option for molecular therapy of hepatocellular carcinoma (HCC). PMID: 27592554
Binding of RS1-Reg to ODC1 inhibits the enzymatic activity at low intracellular glucose, which is blunted at high intracellular glucose. PMID: 27555600
mechanistic study of the molecular interactions between antizyme inhibitor and its interacting proteins CCND1 and ornithine decarboxylase PMID: 26172301
We earlier presented evidence for a physical interaction between ODC and SPR and we showed that RNAi-mediated knockdown of SPR expression significantly reduced native ODC enzyme activity and impeded Neuroblastoma cell proliferation. PMID: 26093909
Bag-1 indirectly affects cell survival through c-Myc activated signalling that causes elevation of ornithine decarboxylase levels, leading to an increase of the polyamine content. PMID: 26178413
High ODC expression is associated with Medulloblastoma. PMID: 26460945
Data suggest that down-regulation of ODC (using siRNA or pharmacologic inhibitor) in bone marrow-derived mesenchymal stem cells results in reduced intracellular polyamines (putrescine, spermidine, and spermine) and enhanced osteogenesis. PMID: 26140984
tumor ornithine decarboxylase level heterogeneity increased with increasing tumor malignancy PMID: 17582600
The results suggested that the ODC gene might act as a prognostic factor for breast cancer and it could be a promising therapeutic target. PMID: 18330478
BTF3, HINT1, NDRG1 and ODC1 protein over-expression in human prostate cancer tissue PMID: 24386364
Akt activation by ODC+COX-2 over-expression. PMID: 24260338
Authors identified SPR as a novel regulator of ODC enzyme activity and, based on clinical evidence, present a model in which SPR drives ODC-mediated malignant progression in neuroblastoma. PMID: 24096079
ODC overexpression suppresses the expression of tumstatin, which may provide fundamental evidence for the combination of anti-angiogenic therapy and conventional therapy for cancer treatment. PMID: 24002681
The results of this study suggest that specific genetic variants in a subset of glutamatergic (GRIN2B) and polyaminergic (ODC1) neurosystem genes may be of importance in certain suicidal subjects. PMID: 22850629
There are five conserved residues in ODC. PMID: 23872168
Based on the investigation of the polyamine metabolite pathway, these data establish that the downstream metabolites of ornithine are increased, potentially implicating ornithine decarboxylase activity in AD pathology. PMID: 23917584
Overexpression of antizyme (AZ), an ornithine decarboxylase (ODC) inhibitory protein, suppressed ERalpha expression, suggesting that ODC plays an important role in regulation of ERalpha expression. PMID: 22976807
Introduction of a fluorine atom at C3 of 3-deazauridine shifts its antimetabolic activity from inhibition of CTP synthetase to inhibition of orotidylate decarboxylase, an early event in the de novo pyrimidine nucleotide biosynthesis pathway. PMID: 22730407
Variants of the ornithine decarboxylase gene influence risk of colorectal adenoma and aspirin chemoprevention. PMID: 21930798
the mechanism of formation of the internal aldimine, a common intermediate to most pyridoxal 5'-phosphate (PLP)-dependent enzymes PMID: 21854048
There was no significant association between ODC G316A and risk of colorectal cancer for either heterozygotes or rare allele homozygotes. PMID: 20456464
Studies provide lead compounds for inhibitors of ornithine decarboxylase and human histidine decarboxylase. PMID: 21454364
Gingival ornithine decarboxylase levels were higher in the gingivitis group compared to the periodontitis and healthy groups at baseline. PMID: 20831369
Overexpression of ODC suppresses thapsigargin-induced apoptosis, blocks caspase-4 activation and PERK phosphorylation,and attenuates CHOP expression. It inhibits Bak increase and maintains Bcl-2 expression, blocking the intrinsic pathway of apoptosis. PMID: 20814750
Ornithine decarboxylase induces hypomethylation of genome DNA and histone H3 lysine 9 dimethylation in human oral cancer cell line. PMID: 20838441
ODC activity, which AZIN2 is assumed to regulate, is strongly associated with cell growth and transformation. PMID: 19832840
Low Ornithine decarboxylase mRNA expression is associated with more aggressive non-small-cell lung cancer. PMID: 20199977
Overexpression of ornithine decarboxylase enhances endothelial proliferation by suppressing endostatin expression. PMID: 11830503
ODC activity reflects aggressive growth and malignization in meningiomas. PMID: 15015770
Data show that expressing whole proteins, protein domains, or peptide ligands fused to the N terminus of ornithine decarboxylase promotes proteasome-dependent degradation of these chimeric fusion proteins and their interacting cellular target proteins. PMID: 16219697
review of key factors that contribute to the regulation of ornithine decarboxylase levels, which can occur at the levels of transcription, translation, and protein turnover [review] PMID: 16459331
findings show that antibody-bound amyloid precursor protein induces expression of ornithine decarboxylase PMID: 16469300
Data suggest that prolaction-mediated induction of ornithine decarboxylase activity enhances expression of Bcl-2 strongly enough to bring about prolactin's anti-apoptotic function. PMID: 16520895
This is the first report showing the existence of a causal relationship between ornithine decarboxylase expression, Erk and p38 MAP kinase activation, and MMP-2 expression. PMID: 17088079
no association observed between the ODC ploymorphism and H. pylori seropositivity; results did not support the hypothesis that the different genetic traits in the ODC-polyamine pathway are associated with susceptibility to persistent H. pylori infection PMID: 17378176
The expression of ornithine decarboxylase is positively correlated with the degree of malignity of gastric mucosa and development of gastric lesions. PMID: 17569126
Among colorectal cancer patients, ODC activity in cancer tissue was correlated with T factors, lymph node metastasis and stages. PMID: 17957960
Antisense RNA specifically inhibited the expression of ODC and AdoMetDC and the synthesis of polyamine, while it induced p21 expression, resulting in cell growth arrest in the G1 phase in prostate cancer cells. PMID: 18548481
Elevated ODC1 (independent of MYCN amplification) was associated with reduced survival in a large independent neuroblastoma cohort. PMID: 19047152
sporadic breast cancer, the presence of at least one A allele in ornithine decarboxylase is protective against the disease. PMID: 19225907
The ODC1 SNP may be protective for colon adenoma recurrence and detrimental for survival after colon cancer diagnosis. PMID: 19789310

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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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