ArfGAP With GTPase Domain, Ankyrin Repeat And PH Domain 1 (AGAP1) Antibody

Este producto es parte de AGAP - Arf-GAP with GTPase ANK repeat and PH domain-containing protein
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357.5€ (100 µg)

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935106861
info@markelab.com
name
ArfGAP With GTPase Domain, Ankyrin Repeat And PH Domain 1 (AGAP1) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx038303
tested applications
ELISA, WB

Description

Rabbit Polyclonal against the AGAP1 protein.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Primary Antibodies
Immunogen Target
ArfGAP With GTPase Domain, Ankyrin Repeat And PH Domain 1 (AGAP1)
Host
Rabbit
Reactivity
Human, Mouse
Recommended Dilution
ELISA: 1/20000 - 1/80000, WB: 1/500 - 1/2000. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Purification
Purified by Protein A/G column chromatography.
Size 1
100 µg
Size 2
1 mg
Form
Lyophilized
Tested Applications
ELISA, WB
Buffer
Prior to lyophilization: 0.02% NaN3.
Availability
Shipped within 7-15 working days.
Storage
Store at -20 °C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
NCBI Accession
NM_001037131.1
Alias
AGAP-1,CENTG2,GGAP1
Background
Antibody anti-AGAP1
Status
RUO
Note
Concentration: Lyophilized form: Not applicable.  After reconstitution: 1 mg/ml. - 

Descripción

AGAP1 is a multifunctional protein involved in regulating endocytic trafficking, cytoskeletal organization, and intracellular signaling. It acts as a GTPase-activating protein (GAP) for Arf family GTPases, facilitating vesicle formation and receptor recycling. Structurally, it contains a GTPase domain, ankyrin repeats for protein-protein interactions, and a PH (pleckstrin homology) domain that enables membrane association. AGAP1 is expressed in various tissues, with high levels in neurons, where it modulates synaptic vesicle trafficking, dendritic spine morphogenesis, and endosomal sorting. Dysregulation of AGAP1 has been linked to neurodevelopmental disorders, cognitive impairments, and cellular transport defects, emphasizing its critical role in neuronal connectivity and function.

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