TP53 Specific Neutra™ Antibody Products

Tumor protein p53, referred to as p53, cellular tumor antigen p53 (designated by UniProt), the Genome Guardian, phosphoprotein p53, tumor suppressor p53, antigen NY-CO-13, or transformation-associated protein 53 (TRP53), denotes any isoform of a protein encoded by conserved genes across different organisms, including TP53 (in humans) and Trp53 (in mice).

Its Gene ID: 7157, UniProtKB ID: P04637, and OMIM ID: 191170.

TP53 Pathway

The TP53 tumor suppressor protein serves as a pivotal obstacle to the onset and advancement of cancer. In terms of mechanisms, TP53 predominantly acts as a transcription factor with specificity to sequences, adhering to distinct DNA segments within the genome and triggering the transcriptional process of nearby genes, alongside remote genes governed by enhancers harboring TP53-binding motifs. Additionally, TP53 possesses the capability to impede the transcription of myriad genes, frequently via indirect pathways.

TP53 primarily serves as a transcription factor to constrain cancer cell proliferation and viability, with numerous non-transcriptional effects also at play. TP53 can facilitate mitochondria-mediated apoptosis by interacting with multi-domain members of the BCL-2 family (e.g., BCL-2 and BCL-X), thereby activating pro-apoptotic BH3-only proteins like BAK and BAX. Additionally, under stress conditions, TP53 can increase cellular Ca2+ levels, leading to apoptosis induction. Moreover, TP53 plays a pivotal role in regulating autophagy.

Fig. 1 p53 exerts a stringent control of the cellular metabolism.¹

Antibodies in TP53-Related Therapeutics

The TP53 protein holds a pivotal position in the orchestration of apoptosis. Dysfunctional TP53 is a prevalent occurrence across numerous cancer types. The utilization of the anti-TP53 antibody is widespread in diverse techniques aimed at cancer therapeutics assays.

• Application of Anti-TP53 in Immunofluorescence Staining

Within cancerous cells, the dysfunctional TP53 protein frequently adopts a misfolded, inert structure stemming from genetic mutations or disturbances in posttranslational modification. These misfolded TP53 variants have the propensity to aggregate, forming amyloid-like oligomers and fibrils that disrupt the pro-apoptotic activities of TP53. Techniques such as immunostaining, western blotting, dot blotting, or ELISA employing antibodies designed to target the conformationally specific epitopes of amyloid fibrils can identify protein aggregates. The polyclonal rabbit antibody (OC), generated through rabbit immunization with Aβ42 fibrils, has the capability to detect both amyloid fibrils and fibrillar oligomers. Utilizing immunofluorescence co-staining with anti-TP53 antibody alongside antibody OC facilitates the visualization of protein aggregates and TP53 protein within cancer cell lines and tumor specimens.

• Function of Anti-TP53 Antibodies in Breast Cancer

Mutation in TP53 is a frequent occurrence in sporadic breast cancer, detected in most invasive carcinomas. The earliest histologic stage where TP53 mutation occurs could be identified using the widely employed anti-TP53 antibody, recognizing both wild type and mutant forms. Immunohistochemical assessment of TP53 expression is conducted in breast carcinomas with known TP53 mutations and adjacent pre-malignant epithelial lesions. Strong nuclear staining for TP53 is observed in tumors harboring missense mutations, contrasting with truncation mutation cases. Intense staining in invasive carcinomas corresponds with similar staining patterns in all ductal carcinoma in situ (DCIS) areas, indicative of missense TP53 mutations. Lighter nuclear staining, potentially indicating elevated levels of normal TP53 protein, is observed in hyperplastic cells and normal breast lobules, irrespective of the mutation type present in invasive carcinoma.

Creative Biolabs offers a diverse range of anti-TP53 antibody offerings, meticulously crafted through recombinant techniques. Furthermore, tailored customization services are accessible to adapt TP53-based bispecific antibodies to precise specifications.

REFERENCE

1. Pitolli, Consuelo, et al. "p53-mediated tumor suppression: DNA-damage response and alternative mechanisms." Cancers 11.12 (2019): 1983. Distributed under Open Access license CC BY 4.0, without modification.