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AB4787

Anti-Rb (phospho T821) antibody

4

(1 Review)

|

(15 Publications)

Rabbit Polyclonal RB phospho T821 antibody. Suitable for WB and reacts with Human samples. Cited in 15 publications. Immunogen corresponding to Synthetic Peptide within Human RB1 phospho T821.

View Alternative Names

Retinoblastoma-associated protein, p105-Rb, p110-RB1, pRb, pp110, Rb, RB1

1 Images
Western blot - Anti-Rb (phospho T821) antibody (AB4787)
  • WB

Unknown

Western blot - Anti-Rb (phospho T821) antibody (AB4787)

Peptide Competition : Cell extracts prepared from Jurkat cells in high growth phase were resolved by SDS-PAGE on a 10% Tris-glycine gel and transferred to PVDF. Membranes were incubated with 0.50 μg/mL ab4787, following prior incubation in the : absence of the phosphopeptide immunogen (1), a generic phosphothreonine containing peptide (2), the non phosphopeptide corresponding to the phosphopeptide immunogen (3), or the presence of the phosphopeptide immunogen (4). After washing, membranes were incubated with goat F(ab’)2 anti-rabbit IgG alkaline phosphatase and bands were detected using the Tropix WesternStar detection method. The data show that only the phosphopeptide corresponding to this site blocks the antibody signal, demonstrating the specificity of the ab4787 antibody for this epitope. Peptide Competition : Cell extracts prepared from Jurkat cells in high growth phase were resolved by SDS-PAGE on a 10% Tris-glycine gel and transferred to PVDF. Membranes were in

All lanes:

Western blot - Anti-Rb (phospho T821) antibody (ab4787)

Predicted band size: 106 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human RB1 phospho T821. The exact immunogen used to generate this antibody is proprietary information.

P06400

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated Rb protein. The final product is generated by affinity chromatography using a Rb-derived peptide that is phosphorylated at threonine 821.
Storage buffer
pH: 7.3 Preservative: 0.05% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Retinoblastoma protein (Rb) also known as pRb is an important regulatory protein with a molecular weight of approximately 110 kDa. It is mainly expressed in the nucleus of cells. Rb functions as a tumor suppressor by controlling the cell cycle progression from G1 to S phase. Rb becomes active when it is dephosphorylated allowing it to bind and inhibit E2F transcription factors consequently preventing the transcription of genes essential for S phase entry.
Biological function summary

Retinoblastoma protein influences cellular proliferation differentiation and apoptosis. It acts within a larger protein complex modulating various cellular responses. When functional Rb halts uncontrolled cell division important for maintaining normal tissue homeostasis. In its phosphorylated state known as phospho-Rb or phospho-Rb E182 it loses its regulatory capabilities which can lead to unrestrained cell cycle progression.

Pathways

Several involve the retinoblastoma protein. One key pathway is the p53 pathway which Rb interacts with to influence cellular outcomes like cell-cycle arrest and apoptosis. Rb cooperates with proteins like p21 to implement these processes. Additionally it is involved in the cyclin D-dependent kinase 4 (CDK4) pathway which modulates its phosphorylation state influencing binding interactions and cell cycle control.

Dysregulation of retinoblastoma protein is commonly associated with cancer particularly retinoblastoma and breast cancer. In retinoblastoma mutations in the Rb gene directly lead to uncontrolled cell proliferation due to the absence of functional Rb protein. Additionally Rb's connection to the E2F family of transcription factors can become disrupted contributing to oncogenesis in other cancers.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed : 10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed : 10499802). Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription (PubMed : 10499802). Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase (PubMed : 10499802). RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C (PubMed : 15084261). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity).. (Microbial infection) In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.
See full target information RB1 phospho T821

Publications (15)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 13:2835 PubMed35595767

2022

Inhibition of the CDK2 and Cyclin A complex leads to autophagic degradation of CDK2 in cancer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Jiawei Zhang,Yichao Gan,Hongzhi Li,Jie Yin,Xin He,Liming Lin,Senlin Xu,Zhipeng Fang,Byung-Wook Kim,Lina Gao,Lili Ding,Eryun Zhang,Xiaoxiao Ma,Junfeng Li,Ling Li,Yang Xu,David Horne,Rongzhen Xu,Hua Yu,Ying Gu,Wendong Huang

Clinical cancer research : an official journal of the American Association for Cancer Research 27:4012-4024 PubMed33879459

2021

Global Phosphoproteomics Reveal CDK Suppression as a Vulnerability to KRas Addiction in Pancreatic Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Aslamuzzaman Kazi,Liwei Chen,Shengyan Xiang,Rajanikanth Vangipurapu,Hua Yang,Francisca Beato,Bin Fang,Terence M Williams,Kazim Husain,Patrick Underwood,Jason B Fleming,Mokenge Malafa,Eric A Welsh,John Koomen,José Trevino,Saïd M Sebti

Breast cancer research : BCR 23:26 PubMed33602273

2021

Distinct mechanisms of resistance to fulvestrant treatment dictate level of ER independence and selective response to CDK inhibitors in metastatic breast cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Kamila Kaminska,Nina Akrap,Johan Staaf,Carla L Alves,Anna Ehinger,Anna Ebbesson,Ingrid Hedenfalk,Lukas Beumers,Srinivas Veerla,Katja Harbst,Sidse Ehmsen,Signe Borgquist,Åke Borg,Alejandro Pérez-Fidalgo,Henrik J Ditzel,Ana Bosch,Gabriella Honeth

Cell cycle (Georgetown, Tex.) 19:2373-2394 PubMed32816597

2020

The PRC2 complex directly regulates the cell cycle and controls proliferation in skeletal muscle.

Applications

Unspecified application

Species

Unspecified reactive species

Abhinav Adhikari,Judith K Davie

Cancer cell 34:626-642.e8 PubMed30300583

2018

The Oncogenic Transcription Factor RUNX1/ETO Corrupts Cell Cycle Regulation to Drive Leukemic Transformation.

Applications

Unspecified application

Species

Unspecified reactive species

Natalia Martinez-Soria,Lynsey McKenzie,Julia Draper,Anetta Ptasinska,Hasan Issa,Sandeep Potluri,Helen J Blair,Anna Pickin,Asmida Isa,Paulynn Suyin Chin,Ricky Tirtakusuma,Daniel Coleman,Sirintra Nakjang,Salam Assi,Victoria Forster,Mojgan Reza,Ed Law,Philip Berry,Dorothee Mueller,Cameron Osborne,Alex Elder,Simon N Bomken,Deepali Pal,James M Allan,Gareth J Veal,Peter N Cockerill,Christian Wichmann,Josef Vormoor,Georges Lacaud,Constanze Bonifer,Olaf Heidenreich

Cellular physiology and biochemistry : internation 48:1382-1396 PubMed30048971

2018

Effects of Fibronectin 1 on Cell Proliferation, Senescence and Apoptosis of Human Glioma Cells Through the PI3K/AKT Signaling Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Yu-Xiang Liao,Zhi-Ping Zhang,Jie Zhao,Jing-Ping Liu

Molecular cancer therapeutics 17:1156-1166 PubMed29545334

2018

ICEC0942, an Orally Bioavailable Selective Inhibitor of CDK7 for Cancer Treatment.

Applications

Unspecified application

Species

Unspecified reactive species

Hetal Patel,Manikandan Periyasamy,Georgina P Sava,Alexander Bondke,Brian W Slafer,Sebastian H B Kroll,Marion Barbazanges,Richard Starkey,Silvia Ottaviani,Alison Harrod,Eric O Aboagye,Laki Buluwela,Matthew J Fuchter,Anthony G M Barrett,R Charles Coombes,Simak Ali

Photochemistry and photobiology 94:589-597 PubMed29143326

2018

LncRNA RP11-670E13.6 Regulates Cell Cycle Progression in UVB Damaged Human Dermal Fibroblasts.

Applications

Unspecified application

Species

Unspecified reactive species

Mengna Li,Li Li,Xiaofeng Zhang,Yan Yan,Baoxi Wang

PloS one 12:e0181601 PubMed28806746

2017

Selective small-chemical inhibitors of protein arginine methyltransferase 5 with anti-lung cancer activity.

Applications

Unspecified application

Species

Unspecified reactive species

Gui-Mei Kong,Min Yu,Zhongping Gu,Zhi Chen,Rui-Ming Xu,Deon O'Bryant,Zhengxin Wang

Scientific reports 6:29417 PubMed27388959

2016

Identification of cyclins A1, E1 and vimentin as downstream targets of heme oxygenase-1 in vascular endothelial growth factor-mediated angiogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Andrea Bauer,Hayley Mylroie,C Clare Thornton,Damien Calay,Graeme M Birdsey,Allan P Kiprianos,Garrick K Wilson,Miguel P Soares,Xiaoke Yin,Manuel Mayr,Anna M Randi,Justin C Mason
View all publications

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