Arf-GAP With GTPase, ANK Repeat And PH Domain-Containing Protein 9 (AGAP9) 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
Arf-GAP With GTPase, ANK Repeat And PH Domain-Containing Protein 9 (AGAP9) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx037412
tested applications
ELISA, WB, IHC

Description

Rabbit Polyclonal against the AGAP9 protein.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Primary Antibodies
Immunogen Target
Arf-GAP With GTPase, ANK Repeat And PH Domain-Containing Protein 9 (AGAP9)
Host
Rabbit
Reactivity
Human
Recommended Dilution
ELISA: 1/20000 - 1/80000, WB: 1/500 - 1/2000, IHC: 1/100 - 1/200. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Purification
Purified by antigen affinity column chromatography.
Size 1
100 µg
Size 2
1 mg
Form
Lyophilized
Tested Applications
ELISA, WB, IHC
Buffer
Prior to lyophilization: 1% BSA and 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_001190810.1
Alias
AGAP-9,CTGLF6
Background
Antibody anti-AGAP9
Status
RUO
Note
Concentration: Lyophilized form: Not applicable.  After reconstitution: 1 mg/ml. - 

Descripción

AGAP9 is a member of the AGAP family, containing characteristic GTPase-activating protein (GAP) domains, ankyrin repeats, and a pleckstrin homology (PH) domain that enable it to regulate Arf GTPases. It is involved in intracellular vesicular trafficking, cytoskeletal reorganization, and membrane dynamics. AGAP9 modulates the activity of small GTPases, which are crucial for endosomal transport, vesicle formation, and cell migration. It is expressed in various tissues, with functional roles in signal transduction and cellular transport mechanisms. Dysregulation of AGAP9 has been implicated in diseases involving defects in intracellular trafficking and cell motility, such as cancer. Its exact mechanisms and clinical implications remain areas of active research.

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