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SAB4200103

Sigma-Aldrich

Anti-AS160 (C-terminal region) antibody produced in rabbit

enhanced validation

~1.5 mg/mL, affinity isolated antibody

Synonym(s):

Anti-Akt substrate of 160 kDa, Anti-TBC1D4 (TBC1 domain family, member 4)

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About This Item

UNSPSC Code:
12352203

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~160 kDa

species reactivity

human

packaging

antibody small pack of 25 μL

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

concentration

~1.5 mg/mL

technique(s)

indirect immunofluorescence: 8-16 μg/mL using HEK-293T cells
western blot: 0.8-1.6 μg/mL using extracts of HEK-293T cells overexpressing human AS160

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TBC1D4(9882)

General description

TBC1 domain family member 4 (TBC1D4) also known AS160, is a protein kinase B (Akt) substrate of 160 kDa. It is a Rab guanine triphosphatase (GTPase)-activating protein (GAP) protein. It consists of two phosphotyrosine-binding (PTB) domains at the N-terminal and a C-terminal catalytic Rab-GAP domain. This multi-domain protein also possesses Akt phosphorylation sites. The AS160 gene is mapped to human chromosome 13q22.2.

Specificity

Anti-AS160 (C-terminal region) specifically recognizes human AS160.

Application

Anti-AS160 (C-terminal region) antibody produced in rabbit may be used in immunoblotting and immunofluorescence.

Biochem/physiol Actions

AS160 protein mediates the translocation of glucose transporter 4 (GLUT4) storage vesicles to the plasma membrane (PM). It is a candidate signaling intermediate, identified as a functional link between the insulin signaling cascade and GLUT4 vesicles. AS160 is known to be phosphorylated by protein kinase B (Akt) on at least six separate sites in response to insulin and is thought to play an inhibitory role in the transport of GLUT4 vesicles. It is associated with GLUT4 vesicles in basal states and dissociates in response to insulin. The inhibitory role of AS160 in the basal state and reduced expression of AS160 in adipocytes has been shown to increase plasma membrane levels of GLUT4 in an insulin-dependent manner. Rab10 has been reported to be a target of AS160, required for insulin-stimulated translocation of GLUT4.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

Store at –20 °C. For continuous use, the product may be stored at 2–8 °C for up to one month. For extended storage, freeze in working aliquots at –20 °C. Repeated freezing and thawing is not recommended. Storage in “frost-free” freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

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.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
Sano H, et al.
The Journal of biological chemistry, 278(17) (2003)
TBC proteins: GAPs for mammalian small GTPase Rab?
Fukuda M
Bioscience Reports, 31(3) (2011)
Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane
Sano H, et al.
Cell Metabolism, 5(4) (2007)
WNK1 phosphorylation sites in TBC1D1 and TBC1D4 modulate cell surface expression of GLUT1
Henriques AFA, et al.
Archives of Biochemistry and Biophysics, 679(4), 108223-108223 (2020)
Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners
Ishiki M and Klip A
Endocrinology, 146(12) (2005)

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