CLONING AND EXPRESSION SOLUBLE RECOMBINANT PARATHYROID HORMONE IN E. COLI

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

AGHAJANI M.H.; TAHZIBI A.; SHAHBAZI M.

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: Journal of Gorgan University of Medical Sciences Year:2016 | Volume:17 | Issue:4 (56) Page(s): 112-118

Download Full-Text

Persian Verion

View:

828

Download:

Cites:

Information Journal Paper

Title

CLONING AND EXPRESSION SOLUBLE RECOMBINANT PARATHYROID HORMONE IN E. COLI

Author(s)

AGHAJANI M.H. | TAHZIBI A. | SHAHBAZI M. | Issue Writer Certificate

Keywords

RECOMBINANT PARATHYROID HORMONEQ2

EXPRESSION VECTORQ2

ENZYMATIC DIGESTIONQ2

PCRQ2

Abstract

Background and Objective: Parathyroid proteins involved in calcium homeostasis. With increasing age and other relevant factors, this hormone is not able to perform its role. Using RECOMBINANT PARATHYROID HORMONE prevent disease progression and effective in improvement of disease. This study was done to design and build the desired construct genes, cloning process and synthesis of soluble parathyroid hormone in E. coli.Methods: In this laboratory study, design and optimization sequence of the gene parathyroid hormone (PTH) was carried out for expression of soluble proteins in bacteria. The construct contining PTH gene (puc 57) transformed into bacteria and cultivation was done in SOB medium then Plasmid extraction was performed. Fragment encoding the PTH was isolated by digestion of the cloning vector and ligate to EXPRESSION VECTOR (PET-32a). Subcloning process followed by induction with IPTG 1mM. The recombinant parathyroid hormon was expressed in bacteria, subsequently.Results: After ENZYMATIC DIGESTION, the fragment encoding the protein of interest was properly localized. The process was confirmed by polymerase chain reaction (PCR). Following performing a transformation, induction process performed by IPTG with final concentration 1mM that caused the soluble parathyroid proteins to be expressed in bacteria and the process was confirmed by Western blot technique.Conclusion: Protein expression in bacteria due to its rapid growth and the need to inexpensive medium is cost-effective. Soluble recombinant protein expression reduces downstream of recombinant protein production.

Cites

No record.

References

No record.

Cite

APA: Copy

AGHAJANI, M.H., TAHZIBI, A., & SHAHBAZI, M.. (2016). CLONING AND EXPRESSION SOLUBLE RECOMBINANT PARATHYROID HORMONE IN E. COLI. JOURNAL OF GORGAN UNIVERSITY OF MEDICAL SCIENCES, 17(4 (56)), 112-118. SID. https://sid.ir/paper/79219/en

Vancouver: Copy

AGHAJANI M.H., TAHZIBI A., SHAHBAZI M.. CLONING AND EXPRESSION SOLUBLE RECOMBINANT PARATHYROID HORMONE IN E. COLI. JOURNAL OF GORGAN UNIVERSITY OF MEDICAL SCIENCES[Internet]. 2016;17(4 (56)):112-118. Available from: https://sid.ir/paper/79219/en

IEEE: Copy

M.H. AGHAJANI, A. TAHZIBI, and M. SHAHBAZI, “CLONING AND EXPRESSION SOLUBLE RECOMBINANT PARATHYROID HORMONE IN E. COLI,” JOURNAL OF GORGAN UNIVERSITY OF MEDICAL SCIENCES, vol. 17, no. 4 (56), pp. 112–118, 2016, [Online]. Available: https://sid.ir/paper/79219/en

Related Journal Papers