ODC1 Human

Ornithine Decarboxylase 1 Human Recombinant
Cat. No.
BT6045
Source
E.coli.
Synonyms
ODC, Ornithine decarboxylase 1, EC 4.1.1.17.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

ODC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 484 amino acids (1-461) and having a molecular mass of 53.5 kDa.
ODC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ornithine decarboxylase is the first and rate-limiting enzyme in the polyamine biosynthesis pathway, catalyzing the conversion of ornithine to putrescine. ODC1, a key enzyme, is involved in various biological processes, including cell growth, transformation, differentiation, and apoptosis. Overexpression of the ODC1 gene plays a crucial role in cell proliferation and cancer development.
Description
Recombinant human ODC1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 484 amino acids (1-461) with a molecular weight of 53.5 kDa. It features a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The ODC1 solution is provided at a concentration of 0.5 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 1 mM DTT, 0.1 M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
ODC, Ornithine decarboxylase 1, EC 4.1.1.17.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNNFGNE EFDCHFLDEG FTAKDILDQK INEVSSSDDK DAFYVADLGD ILKKHLRWLK ALPRVTPFYA VKCNDSKAIV KTLAATGTGF DCASKTEIQL VQSLGVPPER IIYANPCKQV SQIKYAANNG VQMMTFDSEV ELMKVARAHP KAKLVLRIAT DDSKAVCRLS VKFGATLRTS RLLLERAKEL NIDVVGVSFH VGSGCTDPET FVQAISDARC VFDMGAEVGF SMYLLDIGGG FPGSEDVKLK FEEITGVINP ALDKYFPSDS GVRIIAEPGR YYVASAFTLA VNIIAKKIVL KEQTGSDDED ESSEQTFMYY VNDGVYGSFN CILYDHAHVK PLLQKRPKPD EKYYSSSIWG PTCDGLDRIV ERCDLPEMHV GDWMLFENMG AYTVAAASTF NGFQRPTIYY VMSGPAWQLM QQFQNPDFPP EVEEQDASTL PVSCAWESGM KRHRAACASA SINV

Product Science Overview

Gene and Protein Structure

The ODC1 gene is located on chromosome 2p25.1 and encodes a protein that consists of 461 amino acids . The enzyme forms a homodimer, which is necessary for its catalytic activity . The gene has a high turnover rate, meaning it is rapidly synthesized and degraded in response to growth-promoting stimuli .

Biological Function

ODC1 is the rate-limiting enzyme in the polyamine biosynthesis pathway . This pathway is critical for cell growth and differentiation. The enzyme’s activity is tightly regulated, and its expression levels can vary significantly in response to various stimuli, including hormones, growth factors, and oncogenes .

Clinical Significance

Mutations or dysregulation of the ODC1 gene have been associated with several diseases, including colorectal cancer and Bachmann-Bupp Syndrome . The enzyme’s role in cell proliferation makes it a target for cancer research, as inhibiting its activity could potentially slow down the growth of cancer cells .

Recombinant ODC1

Human recombinant ODC1 is produced using recombinant DNA technology, which involves inserting the human ODC1 gene into bacterial or yeast cells to produce the enzyme in large quantities . This recombinant enzyme is used in various research applications, including studying the polyamine biosynthesis pathway and developing potential therapeutic interventions .

Research and Applications

ODC1 is a subject of extensive research due to its critical role in cell growth and proliferation. Researchers are exploring ways to modulate its activity to develop treatments for cancer and other diseases associated with abnormal cell growth . Additionally, the enzyme is used in biochemical assays to study the effects of various compounds on the polyamine biosynthesis pathway .

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