BCL2L12 Protein, Human (GST)

BCL2-like 12 (BCL2L12) is a new member of the apoptosis-related BCL2 gene family. BCL2L12 contains a highly conserved BH2 domain, a BH3-like domain and a proline-rich region. BCL2L12 exhibits pro-apoptotic activity in breast tumor and gastric cancer. BCL2L12 is an inhibitor of post-mitochondrial effector caspase activation, as it binds to and inhibits caspase-7 and upregulates the caspase-3-specific inhibitor 伪B-crystallin (CRYAB). BCL2L12 attenuates endogenous p53-directed transcriptomic changes after genotoxic stress and inhibits p53-dependent DNA damage-induced apoptosis^[1][2]. BCL2L12 Protein, Human (GST) is the recombinant human-derived BCL2L12 protein, expressed by E. coli , with N-GST labeled tag.

Currently, two functional splicing variants of the Bcl2L12 gene are known: one consisting of seven coding exons and producing a 334-amino acid protein with a molecular mass of 36.8 kDa and another one resulting from alternative splicing and giving rise to a protein of 176 amino acids, a splice variant called Bcl2L12A which lacks exon 3 (143 bp). Bcl2L12 interacts with Bcl-xL and Bcl2 in yeast two-hybrid system. Bcl2L12192-220 was a minimal region for Bcl2L12-Bcl-xL interaction. both h1 (L213) and h2 residue (L217) are essential for Bcl2L12 interacting with Bcl2 family proteins^[1].

Human

E. coli

N-GST

Q9HB09-1 (P64-K143)

83596  [NCBI]

Approximately 33 kDa.

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.