Dataset Information

Molecular Characterization and In Silico Analyses of Maurolipin Structure as a Secretory Phospholipase A ₂ (sPLA₂) from Venom Glands of Iranian Scorpio maurus (Arachnida: Scorpionida).

ABSTRACT: The venom is a mixture of various compounds with specific biological activities, such as the phospholipase A ₂ (PLA₂) enzyme present in scorpion venom. PLA₂ plays a key role in inhibiting ryanodine receptor channels and has neurotoxic activity. This study is the first investigation of molecular characterization, cloning, and in silico analyses of PLA₂ from Iranian Scorpio maurus, named Maurolipin. After RNA extraction from S. maurus venom glands, cDNA was synthesized and amplified through RT-PCR using specific primers. Amplified Maurolipin was cloned in TA cloning vector, pTG19. For in silico analyses, the characterized gene was analyzed utilizing different software. Maurolipin coding gene with 432 base pair nucleotide leng

SUBMITTER: Soltan-Alinejad P

PROVIDER: S-EPMC9550507 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

ACCESS DATA

Dataset Information

Molecular Characterization and In Silico Analyses of Maurolipin Structure as a Secretory Phospholipase A ₂ (sPLA₂) from Venom Glands of Iranian Scorpio maurus (Arachnida: Scorpionida).

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

Molecular Characterization and In Silico Analyses of Maurolipin Structure as a Secretory Phospholipase A 2 (sPLA2) from Venom Glands of Iranian Scorpio maurus (Arachnida: Scorpionida).

OmicsDI is part of the ELIXIR infrastructure

Tweets

Molecular Characterization and In Silico Analyses of Maurolipin Structure as a Secretory Phospholipase A ₂ (sPLA₂) from Venom Glands of Iranian Scorpio maurus (Arachnida: Scorpionida).