Lymphokine-activated killer T-cell-originated protein kinase Phospho-Thr9 (PBK pT9) Antibody

221€ (50 µg)
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935106861
info@markelab.com
name
Lymphokine-activated killer T-cell-originated protein kinase Phospho-Thr9 (PBK pT9) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx324582
tested applications
ELISA, WB, IHC
Description
PBK (pT9) Antibody is a Rabbit Polyclonal against PBK (pT9).
Documents del producto
Instrucciones
Data sheet
Product specifications
Category | Primary Antibodies |
Immunogen Target | Lymphokine-activated killer T-cell-originated protein kinase Phospho-Thr9 (PBK pT9) |
Host | Rabbit |
Reactivity | Human |
Assay Data | Modification: Phosphorylation // Target Modification: Thr9 |
Recommended Dilution | ELISA: 1/40000, WB: 1/500 - 1/2000, IHC: 1/100 - 1/300. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Purified by affinity chromatography. |
Size 1 | 50 µg |
Size 2 | 100 µg |
Form | Liquid |
Tested Applications | ELISA, WB, IHC |
Buffer | PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q96KB5 |
Gene ID | 55872 |
Alias | CT84,HEL164,Nori-3,SPK,TOPK,Cancer/testis antigen 84,Spermatogenesis-related protein kinase |
Background | Antibody anti-PBK |
Status | RUO |
Descripción
PDZ Binding Kinase (PBK), also known as TOPK (T-LAK cell-originated protein kinase), is a serine/threonine kinase that is predominantly expressed in proliferating cells and is associated with cell cycle regulation, particularly during the G2/M transition. It is highly active in mitosis, phosphorylating substrates such as histone H3 to regulate chromatin condensation and cell division. PBK is implicated in signaling pathways involving MAPKs and Akt, contributing to cell survival, proliferation, and response to stress stimuli. Overexpression of PBK has been observed in various cancers, including lung, breast, and colorectal cancers, where it promotes oncogenic traits like enhanced proliferation, invasion, and resistance to apoptosis. It has also been linked to the regulation of immune responses, influencing T-cell activation and cytokine production. PBK is tightly regulated through phosphorylation by upstream kinases, such as Cyclin-dependent kinases, and dephosphorylation by phosphatases like PP2A, which ensures its activity is restricted to specific phases of the cell cycle. Its potential as a therapeutic target is being explored due to its limited expression in normal tissues and overexpression in tumors, with inhibitors showing promise in preclinical studies by reducing cancer cell viability and enhancing sensitivity to chemotherapy.
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