Eg5 Antibody [B24B13] | Primary Antibodies

Application: Reactivity: Mouse, Human

Lane 1: Jurkat, Lane 2: NCI-H1975, Lane 3: MCF7, Lane 4: 4T1

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:4000 IF1:50 FCM1:600

Application
WB, IP, IHC, IF, FCM

Reactivity
Mouse, 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
119 kDa

Datasheet & SDS

Biological Description

Specificity
Eg5 Antibody [B24B13] detects endogenous levels of total Eg5 protein.

Clone
B24B13

Synonym(s)
EG5; KNSL1; TRIP5; KIF11; Kinesin-like protein KIF11; Kinesin-like protein 1; Kinesin-like spindle protein HKSP; Kinesin-related motor protein Eg5; Thyroid receptor-interacting protein 5; TR-interacting protein 5; TRIP-5

Background
Eg5 (Kinesin Family Member 11, KIF11) is a homotetrameric, plus-end-directed microtubule motor protein that plays a critical role in assembling bipolar mitotic spindles. Eg5 organizes two motor domains at each end, connected by a central bipolar stalk (containing the bimC box motif) and flexible neck linker regions. These neck linkers enable ATP-dependent conformational changes essential for its motor activity. Conserved motifs such as Loop 8, L11, and L12, along with key residues like R221, coordinate microtubule binding and hydrolysis-coupled stepping. During prophase and prometaphase, Eg5’s tetrameric structure allows it to cross-link and slide antiparallel interpolar microtubules, generating outward forces of approximately 5–7 pN per motor. This force production is achieved through biased, processive 8-nm steps, powered by ATP binding at Walker A/B motifs, which reorient the neck linker to promote movement toward microtubule plus-ends. As a result, Eg5 separates duplicated centrosomes by 5–10 μm and counteracts inward forces from kinesin-14 and dynein, thereby establishing and maintaining spindle bipolarity necessary for proper chromosome congression and segregation. Eg5’s activity is regulated by phosphorylation at T926 and S1033 within its tail domain by CDK1 during the G2/M transition, enhancing its microtubule affinity and activation. Dysregulation of Eg5 leads to monopolar spindle formation, mitotic arrest via spindle assembly checkpoint activation, aneuploidy, and cancer progression, particularly in rapidly proliferating tumors such as breast and hematologic malignancies.

Background

Eg5 (Kinesin Family Member 11, KIF11) is a homotetrameric, plus-end-directed microtubule motor protein that plays a critical role in assembling bipolar mitotic spindles. Eg5 organizes two motor domains at each end, connected by a central bipolar stalk (containing the bimC box motif) and flexible neck linker regions. These neck linkers enable ATP-dependent conformational changes essential for its motor activity. Conserved motifs such as Loop 8, L11, and L12, along with key residues like R221, coordinate microtubule binding and hydrolysis-coupled stepping. During prophase and prometaphase, Eg5’s tetrameric structure allows it to cross-link and slide antiparallel interpolar microtubules, generating outward forces of approximately 5–7 pN per motor. This force production is achieved through biased, processive 8-nm steps, powered by ATP binding at Walker A/B motifs, which reorient the neck linker to promote movement toward microtubule plus-ends. As a result, Eg5 separates duplicated centrosomes by 5–10 μm and counteracts inward forces from kinesin-14 and dynein, thereby establishing and maintaining spindle bipolarity necessary for proper chromosome congression and segregation. Eg5’s activity is regulated by phosphorylation at T926 and S1033 within its tail domain by CDK1 during the G2/M transition, enhancing its microtubule affinity and activation. Dysregulation of Eg5 leads to monopolar spindle formation, mitotic arrest via spindle assembly checkpoint activation, aneuploidy, and cancer progression, particularly in rapidly proliferating tumors such as breast and hematologic malignancies.

References
https://pubmed.ncbi.nlm.nih.gov/34203964/ https://pubmed.ncbi.nlm.nih.gov/31958056/

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%