Recombinant Mouse Arpin Protein, Myc/DDK-tagged

• Cat.No.: Arpin-1728M
• Product Overview: Purified recombinant protein of mouse full-length actin-related protein 2/3 complex inhibitor (Arpin), with C-terminal MYC/DDK tag, expressed in HEK293T cells.

Specification

• Description: Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence.
• Source: HEK293T
• Species: Mouse
• Tag: Myc/DDK
• Molecular Mass: 25.2 kDa
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
• Storage: Store at -80 centigrade after receiving vials.
• Concentration: >50 μg/mL as determined by microplate BCA method
• Storage Buffer: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol.

Gene Information

• Gene Name: Arpin actin-related protein 2/3 complex inhibitor [ Mus musculus (house mouse) ]
• Official Symbol: Arpin
• Synonyms: Arpin; actin-related protein 2/3 complex inhibitor; 2610034B18Rik; arpin; UPF0552 protein C15orf38 homolog; arp2/3 inhibition protein
• Gene ID: 70420
• mRNA Refseq: NM_027420
• Protein Refseq: NP_081696
• UniProt ID: Q9D0A3

Reviews

04/01/2021

This cutting-edge technique allows for the visualization and characterization of protein structures at the atomic level, providing insights into their function and potential therapeutic targets.

06/30/2020

Its exceptional performance in ELISA assays makes it a reliable tool for detecting and quantifying specific target molecules with high sensitivity and specificity.

05/12/2017

the ARPIN protein has demonstrated its efficacy in protein electron microscopy structure analysis.

Q&As

Is ARPIN evolutionarily conserved across different species?

Yes, ARPIN is conserved in various species, including mammals, birds, reptiles, and even some invertebrates. This conservation suggests that it plays an important role in regulating actin cytoskeleton dynamics throughout evolution.

What role does ARPIN play in cell migration?

ARPIN plays a crucial role in regulating cell migration. By inhibiting the Arp2/3 complex, it reduces the formation of branched actin networks at the leading edge of migrating cells. This influences the organization of the actin cytoskeleton, lamellipodia formation, and overall cell motility.

Are there any known interacting proteins of ARPIN?

Yes, several proteins have been identified as interacting partners for ARPIN. These include the Arp2/3 complex, which is the main target of ARPIN's inhibitory action, as well as other actin-binding proteins and signaling molecules involved in actin dynamics regulation. Examples of interacting proteins include WASP, WAVE, cortactin, and cofilin.

Can changes in ARPIN expression levels affect the overall actin cytoskeleton organization?

Yes, changes in ARPIN expression levels can influence actin cytoskeleton organization. Overexpression of ARPIN leads to reduced actin branching, resulting in altered actin filament architecture and cell morphology. On the other hand, decreased ARPIN expression or activity may promote excessive actin polymerization and branching, affecting cellular processes that rely on proper actin cytoskeleton dynamics.

Are there any diseases or disorders associated with ARPIN dysfunction?

While not extensively studied, dysregulation of ARPIN has been proposed to contribute to various pathological conditions. Altered expression or activity of ARPIN has been implicated in cancer metastasis, neuronal development disorders, and immune cell dysfunction, among others.

Can ARPIN be targeted for therapeutic interventions in diseases?

The potential therapeutic targeting of ARPIN is an area of active research. Modulating the activity of ARPIN could have implications for diseases such as cancer, where disruption of actin dynamics is frequently observed. However, more studies are needed to evaluate the feasibility and effectiveness of targeting ARPIN for therapeutic purposes.