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Key Documents

SAB2100143

Sigma-Aldrich

Anti-ARF1 antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-ADP-ribosylation factor 1

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About This Item

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

21 kDa

species reactivity

mouse, human, guinea pig, rat, yeast, sheep, dog, rabbit, horse, bovine

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ARF1(375)

Related Categories

General description

Adenosine diphosphate ribosylation factor 1 (ARF1) protein belongs to the class I ARF family of proteins. This protein is present in the Golgi apparatus. The ARF1 gene is located on the human chromosome at 1q42.13.

Immunogen

Synthetic peptide directed towards the middle region of human ARF1

Application

Anti-ARF1 antibody produced in rabbit has been used in western blotting.

Biochem/physiol Actions

Adenosine diphosphate ribosylation factor 1 (ARF1) plays a role in mediating retrograde and anterograde vesicular traffic. This protein also plays a role in the synthesis of coat protein I (COP-I) coated vesicles. ARF1 is involved in the recruitment of clathrin adaptor complexes such as activator protein 1, 3, and 4. The activation of ARF1 triggers the assembly of spectrin as well as actin cytoskeleton in the Golgi membranes.

Sequence

Synthetic peptide located within the following region: MRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQA

Physical form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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 Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Crislyn D'Souza-Schorey et al.
Nature reviews. Molecular cell biology, 7(5), 347-358 (2006-04-25)
The ADP-ribosylation factor (ARF) small GTPases regulate vesicular traffic and organelle structure by recruiting coat proteins, regulating phospholipid metabolism and modulating the structure of actin at membrane surfaces. Recent advances in our understanding of the signalling pathways that are regulated
Julie G Donaldson et al.
Nature reviews. Molecular cell biology, 12(6), 362-375 (2011-05-19)
Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotide-binding (G) proteins, including the ARF-like (ARL) proteins and SAR1, regulate membrane traffic and organelle structure by recruiting cargo-sorting coat proteins, modulating membrane lipid composition, and interacting with regulators of other G
Yoshimi Ohashi et al.
The Journal of biological chemistry, 287(6), 3885-3897 (2011-12-14)
ADP-ribosylation factor 1 (Arf1) plays a major role in mediating vesicular transport. Brefeldin A (BFA), a known inhibitor of the Arf1-guanine nucleotide exchange factor (GEF) interaction, is highly cytotoxic. Therefore, interaction of Arf1 with ArfGEF is an attractive target for
Zhe Sun et al.
Traffic (Copenhagen, Denmark), 8(5), 582-593 (2007-04-25)
The small GTPase ADP-ribosylation factor-1 (Arf1) plays a key role in the formation of coat protein I (COP I)-coated vesicles. Upon recruitment to the donor Golgi membrane by interaction with dimeric p24 proteins, Arf1's GDP is exchanged for GTP. Arf1-GTP
Transcriptional features of multiple myeloma patients with chromosome 1q gain.
S Fabris et al.
Leukemia, 21(5), 1113-1116 (2007-02-23)

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