Arf-GAP With Coiled-Coil, ANK Repeat And PH Domain Containing Protein 1 (ACAP1) Antibody

357.5€ (100 µg)
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935106861
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name
Arf-GAP With Coiled-Coil, ANK Repeat And PH Domain Containing Protein 1 (ACAP1) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx122383
tested applications
ELISA, WB
Description
Rabbit Polyclonal against the ACAP1 protein.
Documents del producto
Instrucciones
Data sheet
Product specifications
Category | Primary Antibodies |
Immunogen Target | Arf-GAP With Coiled-Coil, ANK Repeat And PH Domain Containing Protein 1 (ACAP1) |
Host | Rabbit |
Reactivity | Human |
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 antigen affinity column chromatography. |
Size 1 | 100 µg |
Size 2 | 1 mg |
Form | Lyophilized |
Tested Applications | ELISA, WB |
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 | BC018543 |
Alias | CENTB1,Centaurin beta 1 |
Background | Antibody anti-ACAP1 |
Status | RUO |
Note | Concentration: Lyophilized form: Not applicable. After reconstitution: 1 mg/ml. - |
Descripción
ACAP1 is a multifunctional protein that acts as a GTPase-activating protein (GAP) for ADP-ribosylation factors (Arfs), small GTP-binding proteins involved in vesicle trafficking and membrane dynamics. It contains a pleckstrin homology (PH) domain, ankyrin repeats, and a coiled-coil region, enabling interactions with phospholipids and proteins. ACAP1 is involved in clathrin-mediated endocytosis and recycling of membrane proteins like integrins and nutrient receptors, regulating cellular adhesion, migration, and nutrient uptake. It plays a significant role in immune and migrating cells by recycling surface proteins critical for cellular responses. Dysregulation of ACAP1 has been linked to impaired membrane trafficking, contributing to diseases such as cancer and immune disorders.
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