Arf-GAP With GTPase, ANK Repeat And PH Domain-Containing Protein 4 (AGAP4) Antibody

Este producto es parte de AGAP - Arf-GAP with GTPase ANK repeat and PH domain-containing protein
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292.5€ (80 µl)

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935106861
info@markelab.com
name
Arf-GAP With GTPase, ANK Repeat And PH Domain-Containing Protein 4 (AGAP4) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx027510
tested applications
ELISA, WB

Description

AGAP4 is putative GTPase-activating protein (Potential).

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
Arf-GAP With GTPase, ANK Repeat And PH Domain-Containing Protein 4 (AGAP4)
Host
Rabbit
Reactivity
Human
Recommended Dilution
WB: 1/1000. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Purification
Purified through a protein A column, followed by peptide affinity purification.
Size 1
80 µl
Size 2
400 µl
Form
Liquid
Tested Applications
ELISA, WB
Buffer
PBS containing 0.09% sodium azide.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
Q96P64
Alias
AGAP-4,AGAP-8,AGAP8
Background
Antibody anti-AGAP4
Status
RUO

Descripción

AGAP4 is a member of the AGAP protein family involved in intracellular vesicular transport, membrane trafficking, and the regulation of the actin cytoskeleton. It contains domains similar to other AGAP family members, including a GAP domain, ankyrin repeats, and a PH domain, which enable it to act as a mediator of Arf GTPase activity. AGAP4 is expressed across multiple tissues and is implicated in processes such as endocytic recycling, vesicle sorting, and signal transduction. While its biological roles are less defined compared to other AGAP proteins, emerging studies suggest its involvement in modulating cell adhesion and migration. Altered AGAP4 expression may contribute to tumor progression, especially in cancers where vesicular trafficking and cytoskeletal remodeling are dysregulated.

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