Anti-NCAPG2 antibody

• IP

Supplier Data

Immunoprecipitation - Anti-NCAPG2 antibody (AB70350)

ab70350 immunoprecipitating NCAPG2 at 6 µg per reaction. Lane 1 : ab70350 in HeLa whole cell extract (0.5 or 1 mg per IP reaction; 20% of IP loaded). Lane 2 : IgG control. For blotting immunoprecipitated NCAPG2, ab70350 was used at 1 µg/mL. Detection : Chemiluminescence with an exposure time of 30 seconds.

All lanes:

Immunoprecipitation - Anti-NCAPG2 antibody (ab70350)

Predicted band size: 131 kDa

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• WB

Unknown

Western blot - Anti-NCAPG2 antibody (AB70350)

All lanes:

Western blot - Anti-NCAPG2 antibody (ab70350) at 0.04 µg/mL

Lane 1:

HeLa whole cell lysate at 50 µg

Lane 2:

HeLa whole cell lysate at 15 µg

Lane 3:

HeLa whole cell lysate at 5 µg

Predicted band size: 131 kDa

Observed band size: 131 kDa

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• WB

CiteAb

Western blot - Anti-NCAPG2 antibody (AB70350)

NCAPG2 western blot using anti-NCAPG2 antibody ab70350. Publication image and figure legend from Deutschman, E., Ward, J. R., et al., 2019, J Cell Sci, PubMed 31653782.

ab70350 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab70350 please see the product overview.

NCAPH2 and SMC2 localize to mitochondria in human cells, while NCAPG2 does not. (A) Equal amounts of mitochondrial and cytoplasmic lysates were isolated from equal numbers of NT and NCAPH2 shRNA-expressing cells. HT-29 cells were immunoblotted with antibodies targeting NCAPH2. Immunoblot with antibodies against complex V and β-tubulin are shown to confirm the identity of mitochondrial and cytoplasmic fractions, respectively. NCAPH2 band intensities were normalized to the respective loading controls. NCAPH2 levels in isolated fractions from NCAPH2 shRNA-expressing cells were compared to levels in NT shRNA fractions, which were set to 100%. A representative of two independent experiments is shown. (B) Equal amounts of mitochondrial and cytoplasmic lysates were isolated from equal numbers of NT and NCAPG2 shRNA-expressing cells. HT-29 cells were immunoblotted with antibodies targeting NCAPG2. Immunoblot with antibodies against complex V and β-tubulin are shown to confirm the identity of mitochondrial and cytoplasmic fractions, respectively. NCAPG2 band intensities were normalized to the respective loading controls. NCAPG2 levels in isolated fractions from NCAPG2 shRNA-expressing cells were compared to levels in NT shRNA fractions, which were set to 100%. A representative of two independent experiments is shown. (C) Equal amounts of mitochondrial and cytoplasmic lysates were isolated from equal numbers of NT and SMC2 shRNA-expressing HT-29 cells immunoblotted with antibodies targeting SMC2. Immunoblot with antibodies against complex V and β-tubulin are shown to confirm the identity of mitochondrial and cytoplasmic fractions, respectively. SMC2 band intensities were normalized to the respective loading controls. SMC2 levels in isolated fractions from SMC2 shRNA-expressing cells were compared to levels in NT shRNA fractions, which were set to 100%. A representative of two independent experiments is shown.

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