Recombinant Rat ARPC1A Protein Pre-coupled Magnetic Beads

• Cat.No.: ARPC1A-453R-B
• Product Overview: The Recombnant protein was conjugated to magnetic beads. This ready-to-use, pre-coupled magnetic beads are in uniform particle size and narrow size distribution with large surface area, which is conducive to convenient and fast capture target molecules with high specificity and achieve magnetic separation. This product can be equipped with automation equipment for high-throughput operations.

Specification

• Source: HEK293
• Species: Rat
• Form: Solution
• Particle size: ~2 μm
• Beads Surface: Hydrophilic
• Capacity: > 200 pmol rabbit IgG/ mg beads
• Applications: Immunoassay, In vitro diagnostics, cell sorting, Immunoprecipitation/Co-precipitation, Protein/antibody separation and purification.
• Stability: Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions.
• Storage: 2-8℃. Do not to freeze thaw the Beads
• Concentration: 10mg beads/mL
• Storage Buffer: PBS buffer

Gene Information

• Gene Name: Arpc1a actin related protein 2/3 complex, subunit 1A [ Rattus norvegicus ]
• Official Symbol: ARPC1A
• Gene ID: 81824
• mRNA Refseq: NM_031146.2
• Protein Refseq: NP_112408.1
• UniProt ID: Q99PD4

Reviews

04/14/2023

Their dedicated team of experts is prompt, knowledgeable, and readily available to tackle any hurdles or concerns I may encounter.

12/13/2022

Used in protein electron microscopy structure analysis.Great.

11/11/2019

The ARPC1A protein showcases unparalleled quality, ensuring it surpasses expectations and satisfactorily addresses my experimental requirements.

Q&As

Are there any known post-translational modifications of the ARPC1A protein?

Yes, the ARPC1A protein can undergo post-translational modifications, including phosphorylation and acetylation, which may regulate its activity and interactions with other proteins. The specific effects and functional significance of these modifications are still being studied.

Can the ARPC1A protein form complexes with other protein families apart from the Arp2/3 complex?

Yes, in addition to its association with the other subunits of the Arp2/3 complex, the ARPC1A protein can interact with various actin-binding proteins and regulatory factors. For example, it can associate with WASP (Wiskott-Aldrich syndrome protein) family members, which play a crucial role in actin cytoskeleton regulation.

What are the structural features of the ARPC1A protein?

The ARPC1A protein consists of multiple domains that are involved in protein-protein interactions. It has a predicted alpha-helical coiled-coil domain near the N-terminus, which mediates interactions with other subunits of the Arp2/3 complex. The C-terminus of ARPC1A contains an actin-binding-like domain (ABD) that helps anchor the complex to newly polymerized actin filaments.

Are there any known interacting partners of the ARPC1A protein?

The ARPC1A protein interacts with other subunits of the Arp2/3 complex, such as ARPC1B, ARPC2, and ARPC5, to form the functional complex. It also interacts with various actin-binding proteins, regulatory proteins, and signaling molecules that help regulate actin polymerization and participate in specific cellular processes.

Is the ARPC1A protein expressed in all cell types?

Yes, the ARPC1A protein is expressed in most, if not all, cell types. Actin filament nucleation and branching are essential processes for various cellular functions, so the ARPC1A protein is required in a wide range of cell types and tissues.

Are there any known diseases or disorders associated with ARPC1A protein dysfunction?

Yes, mutations in the ARPC1A gene have been linked to a rare genetic disorder called ARPC1A-related intellectual disability, which is characterized by developmental delay, intellectual disability, and distinctive facial features. These mutations can disrupt the normal function of the ARPC1A protein, impairing actin filament nucleation and branching processes.

How is the ARPC1A protein regulated in cells?

The activity and expression of the ARPC1A protein can be regulated in multiple ways. It can be regulated at the transcriptional level through various transcription factors and signaling pathways. Post-translational modifications, such as phosphorylation and acetylation, can also regulate its activity. Additionally, the availability of other subunits of the Arp2/3 complex can influence the assembly and stability of the complex, thereby affecting ARPC1A function.