OAZ1 Human

Ornithine Decarboxylase Antizyme 1 Human Recombinant
Cat. No.
BT2342
Source
E.coli.
Synonyms
Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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

OAZ1 Human Recombinant produced in E. coli is a single polypeptide chain containing 251 amino acids (1-228) and having a molecular mass of 27.8 kDa.
OAZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
As a member of the ODC antizyme family, OAZ1 plays a crucial role in regulating polyamine synthesis. Its expression is self-regulated through a process called polyamine-enhanced translational frameshifting. OAZ1 acts as a negative regulator of polyamine production by enhancing the negative feedback loop that controls ornithine decarboxylase (ODC) activity. This protein effectively inhibits ODC and accelerates its degradation.
Description
Recombinant OAZ1 Human, produced in E. coli, is a single polypeptide chain with a molecular weight of 27.8 kDa. It comprises 251 amino acids, specifically amino acids 1-228. The protein is engineered with a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
The product is a sterile, filtered solution that appears colorless.
Formulation
The OAZ1 solution is provided at a concentration of 0.25mg/ml. The solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, and 30% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To further enhance long-term stability, consider adding a carrier protein such as 0.1% HSA or BSA. It is crucial to avoid repeated freeze-thaw cycles to maintain product integrity.
Purity
The purity of the product is determined to be greater than 90% based on SDS-PAGE analysis.
Synonyms
Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVKSSLQ RILNSHCFAR EKEGDKPSAT IHASRTMPLL SLHSRGGSSS ESSRVSLHCC SNPGPGPRWC SDAPHPPLKI PGGRGNSQRD HNLSANLFYS DDRLNVTEEL TSNDKTRILN VQSRLTDAKR INWRTVLSGG SLYIEIPGGA LPEGSKDSFA VLLEFAEEQL RADHVFICFH KNREDRAALL RTFSFLGFEI VRPGHPLVPK RPDACFMAYT FERESSGEEE E

Product Science Overview

Structure and Mechanism

OAZ1 is unique in its regulation mechanism, which involves a programmed ribosomal frameshift during its translation. This frameshift is induced by high levels of polyamines, leading to the production of the full-length antizyme protein . Once synthesized, OAZ1 binds to ODC, promoting its degradation by the 26S proteasome, thus reducing polyamine synthesis .

Biological Functions

OAZ1 is not only involved in polyamine regulation but also plays a role in various cellular processes:

  • Cell Growth and Proliferation: By controlling polyamine levels, OAZ1 indirectly influences cell growth and proliferation .
  • Differentiation and Apoptosis: OAZ1 has been implicated in cellular differentiation and programmed cell death, highlighting its importance in maintaining cellular homeostasis .
Recombinant OAZ1

Recombinant OAZ1 is produced using genetic engineering techniques, where the OAZ1 gene is cloned and expressed in suitable host cells, such as E. coli or mammalian cells. This recombinant protein is used in research to study its function and potential therapeutic applications.

Research and Applications

Recent studies have shown that knocking out OAZ1 in human embryonic kidney (HEK293) cells can significantly increase recombinant protein expression . This finding suggests that OAZ1 could be a potential target for improving the production of therapeutic proteins in biopharmaceutical industries.

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