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Merck

A3231

Sigma-Aldrich

Anti-ATG3 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-APG3, Anti-APG3L, Anti-Autophagy related 3 homolog (S. cerevisiae), Anti-DKFZp564M1178, Anti-FLJ22125, Anti-MGC15201, Anti-PC3-96

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~36 kDa

species reactivity

human, mouse, rat

technique(s)

immunoprecipitation (IP): 5-10 μL using rat NRK cell lysate
western blot: 2-4 μg/mL using whole extracts of human HeLa and mouse 3T3 cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ATG3(64422)
mouse ... Atg3(67841)

Categorías relacionadas

General description

ATG3 is a member of the autophagy-related protein family and is involved in the formation of the autophagosome.
Autophagy-related protein 3 (ATG3) is a member of the autophagy-related protein family. It is a mammalian homolog of yeast Apg3p/ Atg3 is ubiquitously expressed in human tissues.

Immunogen

synthetic peptide corresponding to amino acids 17-32 of human Atg3, conjugated to KLH via a C-terminal cysteine residue. The corresponding sequence is identical in rat and mouse.

Application

Anti-ATG3 antibody produced in rabbit has been used in western blotting and immunoprecipitation.

Biochem/physiol Actions

Autophagy-related protein 3 (ATG3) is involved in the formation of the autophagosome. the mammalian homolog of yeast Apg3p/Aut1p, is an E2-like enzyme that catalyzes the conjugation reaction between Atg8 and phosphatidylethanolamine (PE). Golgi-associated ATPase enhancer of 16 kDa (GATE-16), GABAA receptor-associated protein (GABARAP), and microtubule-associated protein light chain 3 (MAP-LC3) are substrates for Atg3. MAP-LC3 is the preferred substrate. Atg3 interacts with Atg7 to form an E1-E2 complex, and with Atg12, which is a substrate for Atg7 but not for Atg3. Moreover, overexpression of Atg3 facilitates the formation of the Atg12-Atg5 conjugate.

Physical form

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

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

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

The transcription and translation landscapes during human cytomegalovirus infection reveal novel host-pathogen interactions
Tirosh O, et al.
PLoS Pathogens, 11(11), e1005288-e1005288 (2015)
Structural basis of ATG3 recognition by the autophagic ubiquitin-like protein ATG12
Metlagel Z, et al.
Proceedings of the National Academy of Sciences of the USA, 110(47), 18844-18849 (2013)
ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late endosome function
Murrow L, et al.
Nature Cell Biology, 17(3), 300-300 (2015)
Human ATG4 autophagy proteases counteract attachment of ubiquitin-like LC3/GABARAP proteins to other cellular proteins
Agrotis A, et al.
The Journal of Biological Chemistry, 294(34), 12610-12621 (2019)
Lyndsay Murrow et al.
Nature cell biology, 17(3), 300-310 (2015-02-17)
The ubiquitin-like molecule ATG12 is required for the early steps of autophagy. Recently, we identified ATG3, the E2-like enzyme required for LC3 lipidation during autophagy, as an ATG12 conjugation target. Here, we demonstrate that cells lacking ATG12-ATG3 have impaired basal

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