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Anti-phospho-Acetyl CoA Carboxylase (Ser79) Antibody, clone BK102

clone BK102, Upstate®, from mouse

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eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

BK102, monoclonal

species reactivity

rat, mouse

manufacturer/tradename

Upstate®

technique(s)

western blot: suitable

isotype

IgG1λ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

phosphorylation (pSer79)

Gene Information

mouse ... Acaca(107476)

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This Item
05-64505-109807-303
antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified antibody

clone

BK102, monoclonal

clone

JBW502, monoclonal

clone

7D2.2, monoclonal

clone

polyclonal

species reactivity

rat, mouse

species reactivity

human

species reactivity

human, rat

species reactivity

canine, human

manufacturer/tradename

Upstate®

manufacturer/tradename

Upstate®

manufacturer/tradename

-

manufacturer/tradename

Upstate®

technique(s)

western blot: suitable

technique(s)

western blot: suitable

technique(s)

western blot: suitable

technique(s)

western blot: suitable

Specificity

Recognizes phosphorylated Acetyl CoA Carboxylase (Ser79).

Immunogen

Synthetic peptide corresponding to rat Acetyl CoA Carboxylase

Application

Detect phospho-Acetyl CoA Carboxylase (Ser79) using this Anti-phospho-Acetyl CoA Carboxylase (Ser79) Antibody, clone BK102 validated for use in WB.
Research Category
Signaling
Research Sub Category
Insulin/Energy Signaling

Quality

Routinely evaluated by immunoblot on HeLa acid extracts

Target description

257 kDa

Physical form

Format: Purified
Protein A Purified immunoglobulin in 0.1M Tris-Glycine, 0.15M NaCl and 0.05% sodium azide, pH 7.4.
Protein G Purified

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
Acid extracts of HeLa cells

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Zhi-Ping Chen et al.
Diabetes, 52(9), 2205-2212 (2003-08-28)
The effect of exercise intensity on skeletal muscle AMP-activated protein kinase (AMPK) signaling and substrate metabolism was examined in eight men cycling for 20 min at each of three sequential intensities: low (40 +/- 2% VO(2) peak), medium (59 +/-
Tatyana G Kahn et al.
PLoS genetics, 10(7), e1004495-e1004495 (2014-07-11)
Polycomb Group (PcG) proteins are epigenetic repressors that control metazoan development and cell differentiation. In Drosophila, PcG proteins form five distinct complexes targeted to genes by Polycomb Response Elements (PREs). Of all PcG complexes PhoRC is the only one that
Z P Chen et al.
American journal of physiology. Endocrinology and metabolism, 279(5), E1202-E1206 (2000-10-29)
AMP-activated protein kinase (AMPK) is a metabolic stress-sensing protein kinase responsible for coordinating metabolism and energy demand. In rodents, exercise accelerates fatty acid metabolism, enhances glucose uptake, and stimulates nitric oxide (NO) production in skeletal muscle. AMPK phosphorylates and inhibits
B E Kemp et al.
Trends in biochemical sciences, 24(1), 22-25 (1999-03-24)
The AMP-activated protein kinase (AMPK) is a member of a metabolite-sensing protein kinase family that is found in all eukaryotes. AMPK activity is regulated by vigorous exercise, nutrient starvation and ischemia/hypoxia, and modulates many aspects of mammalian cell metabolism. The
Glenn K McConell et al.
The Journal of physiology, 598(18), 3859-3870 (2020-06-27)
AMP-activated protein kinase (AMPK) is considered a major regulator of skeletal muscle metabolism during exercise. However, we previously showed that, although AMPK activity increases by 8-10-fold during ∼120 min of exercise at ∼65% V ̇ O 2 peak

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