p53 (1-342) C-terminal deletion human

NA.26

Human p53 protein is composed of 393 amino acid residues with several distinct regions. The N-terminal activation domain allows p53 protein to recruit the basal transcription machinery and activate the expression of target genes. The core domain binds to target DNA in a sequence-specific manner and the majority of mutations found in human tumors occur in the region of the gene encoding this domain. The C-terminal domain is composed of predominantly basic residues and modification of the C-terminal basic domain, including acetylation, glycosylation and phosphorylation, is an essential mechanism for regulating p53 function. Disruption or loss of oligomerization function is associated with loss of cell cycle arrest. This mutant protein (with the deletion of the C-terminus 51 residues including the entire basic domain and a portion of the tetramerization domain) can be used as a unique tool to study specific functions of p53 related to the C-terminus.

Clear and colorless frozen liquid solution

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

human

expressed in insect cells

≥80% (SDS-PAGE)

frozen liquid

~39.5 kDa

pkg of 5 μg

250 μg/mL

clear colorless

NM_000546

P04637

dry ice

−70℃

human ... TP53(7157)

10 - Combustible liquids

WGK 1