CDKN1A Antibodies

Structure of CDKN1A

The molecular weight of CDKN1A (p21) protein is approximately 21.1 kDa. This value varies among different species, mainly due to its amino acid composition and post-translational modifications.

This protein is composed of 164 amino acids, and its N-terminal domain can bind to multiple cyclin-dependent kinase (CDK) complexes, thereby inhibiting their activity. Its C-end is involved in regulating the processes of cell proliferation and apoptosis. The secondary structure is mainly α -helical, and the key functional region is located at amino acid residues 17 to 24. This region is crucial for its binding and inhibition of the CDK2-cyclin E complex.

Fig. 1 Structure and interactors of CDKN1A/p21.¹

Key structural properties of CDKN1A:

• Contains a conserved N-terminal kinase inhibitory domain
• Extensive binding to a variety of cyclin-cyclin-CDK complexes through this domain
• The C terminal areas involved in regulating the cell positioning and protein stability

Functions of CDKN1A

The core function of the CDKN1A (p21) protein is to act as a key negative regulatory factor in the cell cycle process. However, it is also widely involved in various cellular life activities, including DNA damage responses, cell differentiation and senescence, etc.

The inhibitory effect of CDKN1A on CDK is extensive and non-specific (it can inhibit multiple complexes such as CDK1, CDK2, and CDK4/6), which is different from many more specific CDkis (such as p16), highlighting its fundamental guarding role in maintaining genomic stability.

Applications of CDKN1A and CDKN1A Antibody in Literature

1. Manousakis, Evangelos, et al. "CDKN1A/p21 in Breast Cancer: Part of the Problem, or Part of the Solution?." International Journal of Molecular Sciences 24.24 (2023): 17488. https://doi.org/10.3390/ijms242417488

The article indicates that CDKN1A/p21 is a cell cycle regulatory protein with dual functions, which can both inhibit tumors and potentially promote cancer development. It is involved in processes such as cell proliferation, DNA damage response, tumor stem cell renewal and chemotherapy resistance. Its expression varies among different tumors. Targeted regulation of p21 provides a potential strategy for cancer treatment.

2. Ben-Oz, Bella M., et al. "A dual role of RBM42 in modulating splicing and translation of CDKN1A/p21 during DNA damage response." Nature Communications 14.1 (2023): 7628. https://doi.org/10.1038/s41467-023-43495-6

Research has found that the RBM42 protein maintains genomic stability in DNA damage responses by regulating the expression of CDKN1A/p21. On the one hand, RBM42 promotes the splicing of CDKN1A precursor mRNA and antagonizes the splicing inhibitory function of RBM4. On the other hand, it also participates in regulating the translation process of multiple target genes including CDKN1A, thereby precisely controlling the p21 protein level at the post-transcriptional level.

3. Murphy, Michael R., et al. "Long non-coding RNA generated from CDKN1A gene by alternative polyadenylation regulates p21 expression during DNA damage response." Nucleic Acids Research 51.21 (2023): 11911-11926. https://doi.org/10.1093/nar/gkad899

Research has found that in the DNA damage response, the first intron of the CDKN1A gene undergoes selective polyadenylation (APA), generating an lncRNA named SPUD. SPUD promotes the expression of p21 protein at the translation level by binding to the p21 translation regulatory factors Calreticulin and CUGBP1, thereby influencing the cell cycle process and DNA damage response.

4. Cheng, Wen-Yu, et al. "Polymorphism at codon 31 of CDKN1A (p21) as a predictive factor for bevacizumab therapy in glioblastoma multiforme." BMC cancer 23.1 (2023): 886. https://doi.org/10.1186/s12885-023-11400-5

Research has found that the CDKN1A gene c.93C>A (Ser31Arg) polymorphism is associated with the response to bevacizumab treatment in patients with glioblastoma (GBM). Studies have found that patients carrying the Arg/Arg and Arg/Ser genotypes have more significant survival benefits after receiving bevacizumab combined with chemoradiotherapy. This polymorphism can serve as an early predictor of the efficacy of bevacizumab.

5. Muto, Jun, et al. "Highly concentrated trehalose induces prohealing senescence-like state in fibroblasts via CDKN1A/p21." Communications biology 6.1 (2023): 13. https://doi.org/10.1038/s42003-022-04408-3

Research has found that high-concentration trehalose enhances epidermal expansion and angiogenesis in skin-equivalent models by inducing fibroblast-like senescence, activating the CDKN1A/p21 pathway, and promoting the expression of factors such as DPT and VEGFA, thereby accelerating wound healing in mice. Knockout of CDKN1A can reverse this effect.

Creative Biolabs: CDKN1A Antibodies for Research

Creative Biolabs specializes in the production of high-quality CDKN1A antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom CDKN1A Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our CDKN1A antibodies, custom preparations, or technical support, contact us at email.