Anti-CDKN1A (clone W24V171) Recombinant Antibody Coupled Liposome (VS-1024-FY172) (CAT#: VS-1024-FY172)

• Potential Clinical Applications
• Melanoma

• Clone
• W24V171

• Antibody Type
• IgG1

• Antibody Host
• Mouse

• Antibody Reactivity
• Human

• Antibody Description
• This antibody is a recombinant mouse monoclonal targeting the CDKN1A protein, which is known for its critical role in cell cycle regulation. CDKN1A, also referred to as p21, is a significant inhibitor of cyclin-dependent kinases and serves as a key player in controlling cell proliferation in response to various cellular stresses, including DNA damage and other signals.

• Storage
• See in the COA

• Storage Shelf Time
• See in the COA

• Target
• CDKN1A

• Introduction
• Based on molecular docking results, Ligands-3, 5, 14, and 16 were screened among 17 different Pyrrolone-fused benzosuberene compounds as potent and specific inhibitors without any cross-reactivity against different CDK isoforms. Analysis of MD simulations and MM-PBSA studies, revealed the binding energy profiles of all the selected complexes.

• Alternative Names
• Cyclin Dependent Kinase Inhibitor 1A; Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1); CDK-Interacting Protein 1; CDKN1; CAP20; MDA-6; CIP1; SDI1; WAF1; P21

• Full Name
• Cyclin Dependent Kinase Inhibitor 1A

• Gene ID
• 1026

• UniProt ID
• P38936

• Sequence Similarities
• Belongs to the CDI family.

• Cellular Localization
• Cytoplasm, Nucleus

• Post Translation Modifications
• Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC impairs binding to PCNA. Phosphorylation at Ser-114 by GSK3-beta enhances ubiquitination by the DCX(DTL) complex. Phosphorylation of Thr-145 by PIM2 enhances CDKN1A stability and inhibits cell proliferation. Phosphorylation of Thr-145 by PIM1 results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. UV radiation-induced phosphorylation at Thr-80 by LKB1 and at Ser-146 by NUAK1 leads to its degradation.
  Ubiquitinated by MKRN1; leading to polyubiquitination and 26S proteasome-dependent degradation. Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2) complex, leading to its degradation during S phase or following UV irradiation. Ubiquitination by the DCX(DTL) complex is essential to control replication licensing and is PCNA-dependent: interacts with PCNA via its PIP-box, while the presence of the containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to its degradation. Ubiquitination at Ser-2 leads to degradation by the proteasome pathway. Ubiquitinated by RNF114; leading to proteasomal degradation.
  Acetylation leads to protein stability. Acetylated in vitro on Lys-141, Lys-154, Lys-161 and Lys-163. Deacetylation by HDAC1 is prevented by competitive binding of C10orf90/FATS to HDAC1 (By similarity).

• Protein Refseq
• NP_000380.1; NP_001207706.1; NP_001207707.1

• Function
• May be involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding (PubMed:11595739).
  Plays an important role in controlling cell cycle progression and DNA damage-induced G2 arrest (PubMed:9106657).

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