Aurora A Antibody [J10G23] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:50 IF1:100 - 1:200 FCM1:50 - 1:200

Application
WB, IP, IF, FCM

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
48 kDa

Positive Control	Jurkat cells; HeLa cells; HT-29 cells; HT-29 cells (Thymidine, 2 mM, 17 h; Nocodazole, 100 ng/ml, 24 h)
Negative Control

Datasheet & SDS

Biological Description

Specificity
Aurora A Antibody [J10G23] detects endogenous levels of total Aurora A protein.

Clone
J10G23

Synonym(s)
Aurora kinase A ; Aurora 2; ARK-1); Aurora-related kinase 1; Ipl1- and aurora-related kinase 1; Serine/threonine-protein kinase 15; AURKA; AIK; AIRK1; ARK1; AURA; AYK1; BTAK; IAK1; STK15; STK6

Background
Aurora A (AURKA) is a serine/threonine kinase essential for mitotic fidelity, predominantly localizing to centrosomes and spindle poles to drive cell cycle progression from G2/M through cytokinesis, with its overexpression marking a wide range of epithelial cancers. AURKA features an unstructured N-terminal regulatory domain (39–139 aa), a conserved C-terminal kinase domain (~250–300 aa) composed of N-lobe β-strands and C-lobe α-helices connected by a hinge for conformational flexibility, and a short C-terminal tail, encompassing twelve catalytic subdomains that include the critical activation loop residue Thr288 (site of autophosphorylation, essential for kinase activity but requiring TPX2 allosteric binding for full activation), as well as motifs for ATP binding, Mg²⁺ coordination, and substrate engagement; engineered mutations (C290A/C393A) facilitate crystallographic studies by partially ordering the activation loop. Aurora A’s auto- and trans-phosphorylation at Thr288, coupled with TPX2 binding to a hydrophobic pocket, locks the kinase in the active DFG-in conformation, enabling phosphorylation of downstream targets such as PLK1 (centrosome maturation), TACC3/CKAP5 (microtubule stabilization), LATS2 (G2/M checkpoint), and kinesins Kif2a/Kif2C (spindle dynamics), thereby ensuring accurate bipolar spindle assembly, chromosome alignment, and spindle assembly checkpoint (SAC) satisfaction for timely mitotic progression. Through tight cooperation with Aurora B/C in maintaining kinetochore-microtubule attachments, AURKA safeguards chromosomal stability; dysregulation or amplification disrupts these processes, driving aneuploidy and tumorigenesis in cancer.

Background

Aurora A (AURKA) is a serine/threonine kinase essential for mitotic fidelity, predominantly localizing to centrosomes and spindle poles to drive cell cycle progression from G2/M through cytokinesis, with its overexpression marking a wide range of epithelial cancers. AURKA features an unstructured N-terminal regulatory domain (39–139 aa), a conserved C-terminal kinase domain (~250–300 aa) composed of N-lobe β-strands and C-lobe α-helices connected by a hinge for conformational flexibility, and a short C-terminal tail, encompassing twelve catalytic subdomains that include the critical activation loop residue Thr288 (site of autophosphorylation, essential for kinase activity but requiring TPX2 allosteric binding for full activation), as well as motifs for ATP binding, Mg²⁺ coordination, and substrate engagement; engineered mutations (C290A/C393A) facilitate crystallographic studies by partially ordering the activation loop. Aurora A’s auto- and trans-phosphorylation at Thr288, coupled with TPX2 binding to a hydrophobic pocket, locks the kinase in the active DFG-in conformation, enabling phosphorylation of downstream targets such as PLK1 (centrosome maturation), TACC3/CKAP5 (microtubule stabilization), LATS2 (G2/M checkpoint), and kinesins Kif2a/Kif2C (spindle dynamics), thereby ensuring accurate bipolar spindle assembly, chromosome alignment, and spindle assembly checkpoint (SAC) satisfaction for timely mitotic progression. Through tight cooperation with Aurora B/C in maintaining kinetochore-microtubule attachments, AURKA safeguards chromosomal stability; dysregulation or amplification disrupts these processes, driving aneuploidy and tumorigenesis in cancer.

References
https://pubmed.ncbi.nlm.nih.gov/25760707/ https://pubmed.ncbi.nlm.nih.gov/30250494/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%