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Rabbit Anti-ARF1 Recombinant Antibody (16C10) (CBMAB-A3416-YC)

Provided herein is a Mouse monoclonal antibody against Human ADP Ribosylation Factor 1. The antibody can be used for immunoassay techniques, such as ELISA, WB.
See all ARF1 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
16C10
Antibody Isotype
IgG
Application
IF, WB

Basic Information

Immunogen
A synthetic peptide corresponding to a sequence within amino acids 70-150 of human ARF1.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IF(ICC)1:50-1:200

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.05% BSA, 50% glycerol, pH7.3
Preservative
0.02% sodium azide
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
ADP Ribosylation Factor 1
Introduction
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as
Entrez Gene ID
375
UniProt ID
P84077
Alternative Names
ADP Ribosylation Factor 1;
Function
GTP-binding protein involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).
(Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
Biological Process
Actin filament organization Source: Ensembl
Antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
Ccellular copper ion homeostasis Source: UniProtKB
Cellular response to virus Source: UniProtKB
Dendritic spine organization Source: UniProtKB
Golgi to transport vesicle transport Source: Ensembl
Interleukin-12-mediated signaling pathway Source: Reactome
Intracellular protein transport Source: GO_Central
Long-term synaptic depression Source: UniProtKB
Lysosomal membrane organization Source: Ensembl
Mitotic cleavage furrow ingression Source: Ensembl
Phosphatidylinositol biosynthetic process Source: Reactome
Positive regulation of calcium ion-dependent exocytosis Source: Ensembl
Positive regulation of dendritic spine development Source: Ensembl
Positive regulation of endocytosis Source: Ensembl
Positive regulation of ER to Golgi vesicle-mediated transport Source: Ensembl
Positive regulation of late endosome to lysosome transport Source: Ensembl
Positive regulation of protein secretion Source: Ensembl
Positive regulation of sodium ion transmembrane transport Source: Ensembl
Post-Golgi vesicle-mediated transport Source: Reactome
Postsynaptic actin cytoskeleton organization Source: Ensembl
Regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKB
Regulation of defense response to virus by virus Source: Reactome
Regulation of phospholipid metabolic process Source: Ensembl
Regulation of receptor internalization Source: UniProtKB
Synaptic vesicle budding Source: Ensembl
Very-low-density lipoprotein particle assembly Source: Ensembl
Vesicle-mediated transport Source: GO_Central
Cellular Location
Golgi apparatus; Trans-Golgi network membrane; Perinuclear region; Synaptosome; Postsynaptic density; Membrane
Involvement in disease
Periventricular nodular heterotopia 8 (PVNH8): A form of periventricular nodular heterotopia, a disorder resulting from a defect in the pattern of neuronal migration in which ectopic collections of neurons lie along the lateral ventricles of the brain or just beneath, contiguously or in isolated patches. PVNH8 is an autosomal dominant disease characterized by developmental disabilities, speech delay, seizures and attention deficit hyperactivity disorder.
PTM
Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3.

Feng, H. P., Cheng, H. Y., Hsiao, T. F., Lin, T. W., Hsu, J. W., Huang, L. H., & Yu, C. J. (2021). ArfGAP1 acts as a GTPase‐activating protein for human ADP‐ribosylation factor‐like 1 protein. The FASEB Journal, 35(4), e21337.

Herrera, A., Muroski, J., Sengupta, R., Nguyen, H. H., Agarwal, S., Ogorzalek Loo, R. R., ... & Satchell, K. J. (2020). N‐terminal autoprocessing and acetylation of multifunctional‐autoprocessing repeats‐in‐toxins (MARTX) Makes Caterpillars Floppy‐like effector is stimulated by adenosine diphosphate (ADP)‐Ribosylation Factor 1 in advance of Golgi fragmentation. Cellular microbiology, 22(2), e13133.

Herrera, A., Muroski, J., Sengupta, R., Nguyen, H. H., Agarwal, S., Loo, R. R. O., ... & Satchell, K. J. (2020). N-terminal autoprocessing and acetylation of MARTX Makes-Caterpillars Floppy-like effector is stimulated by ADP-Ribosylation Factor 1 in advance of Golgi fragmentation. Cellular microbiology, 22(2), e13133.

Bansal, A., Kirschner, M., Zu, L., Cai, D., & Zhang, L. (2019). Coconut oil decreases expression of amyloid precursor protein (APP) and secretion of amyloid peptides through inhibition of ADP-ribosylation factor 1 (ARF1). Brain research, 1704, 78-84.

Uchida, R., Egawa, T., Fujita, Y., Furuta, K., Taguchi, H., Tanaka, S., & Nishida, K. (2019). Identification of the minimal region of peptide derived from ADP-ribosylation factor1 (ARF1) that inhibits IgE-mediated mast cell activation. Molecular immunology, 105, 32-37.

Wang, H., Liu, Y., Zhang, L., Kundu, J. K., Liu, W., & Wang, X. (2019). ADP ribosylation factor 1 facilitates spread of wheat dwarf virus in its insect vector. Cellular microbiology, 21(9), e13047.

Dwibhashyam, S. (2019). Expression of a Copper Transporter ADP-ribosylation Factor-1 (Arf1) in the Blood-Cerebrospinal Fluid Barrier.

Xu, X., Wang, Q., He, Y., Ding, L., Zhong, F., Ou, Y., ... & He, S. (2017). ADP-ribosylation factor 1 (ARF1) takes part in cell proliferation and cell adhesion-mediated drug resistance (CAM-DR). Annals of hematology, 96(5), 847-858.

López-Ginés, C., Navarro, L., Muñoz-Hidalgo, L., Buso, E., Morales, J. M., Gil-Benso, R., ... & Cerdá-Nicolás, M. (2017). Association between epidermal growth factor receptor amplification and ADP-ribosylation factor 1 methylation in human glioblastoma. Cellular Oncology, 40(4), 389-399.

Gadahi, J. A., Ehsan, M., Wang, S., Zhang, Z., Yan, R., Song, X., ... & Li, X. (2017). Recombinant protein of Haemonchus contortus small GTPase ADP-ribosylation factor 1 (HcARF1) modulate the cell mediated immune response in vitro. Oncotarget, 8(68), 112211.

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For research use only. Not intended for any clinical use.

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