Recombinant Cynomolgus Monkey AKTIP Protein Pre-coupled Magnetic Beads

• Cat.No.: AKTIP-41C-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: Cynomolgus Monkey
• 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: AKTIP AKT-interacting protein [ Macaca fascicularis (crab-eating macaque) ]
• Official Symbol: AKTIP
• Synonyms: AKTIP; FTS; Fused toes protein homolog
• Gene ID: 101865159
• mRNA Refseq: NM_001284971
• Protein Refseq: NP_001271900
• UniProt ID: Q4R5E1

Reviews

02/07/2021

The AKTIP protein stands as a remarkable solution that exemplifies exceptional quality and meets all my experimental requirements.

06/02/2020

I am confident that the AKTIP protein will unlock vital insights into cellular processes, propelling my scientific investigations to new heights.

07/31/2016

Its impressive purity and functional characteristics make it an ideal choice for my research endeavors, ensuring reliable and impactful results.

05/25/2016

An additional advantage of selecting the AKTIP protein is the outstanding technical support offered by its manufacturer.

Q&As

What are the structural features of AKTIP protein?

The structural features of AKTIP protein have not been extensively characterized. AKTIP contains multiple domains, including an N-terminal pleckstrin homology (PH) domain and a C-terminal coiled-coil domain. The PH domain is known to interact with phospholipids, suggesting a potential role for AKTIP in membrane association. The coiled-coil domain may be involved in protein-protein interactions and the formation of protein complexes.

Are there any known genetic variations or mutations in the AKTIP gene?

Information on genetic variations or mutations in the AKTIP gene is limited. However, genetic variations in AKTIP could potentially exist and contribute to the development of specific diseases. Further research and genetic studies are necessary to investigate potential genetic variations or mutations in the AKTIP gene and their associations with diseases or phenotypic traits.

Are there any inhibitors or activators known for AKTIP protein?

Currently, there have been no specific inhibitors or activators developed for AKTIP protein. However, targeting AKT, the protein that interacts with AKTIP, has been the focus of drug development in various diseases. Small molecule inhibitors of AKT kinase activity, such as MK-2206 and AZD5363, have been developed and are being evaluated in clinical trials. It's possible that targeting AKT could indirectly affect AKTIP function, but direct modulation of AKTIP itself will require further research and development.

What are the potential therapeutic implications of targeting AKTIP protein?

Targeting AKTIP protein or its interaction with AKT could have therapeutic implications in diseases where dysregulation of AKT signaling is involved. Modulating AKTIP's function could potentially impact AKT activity and cellular processes regulated by AKT, such as cell growth, survival, and metabolism. However, further research is needed to fully understand the therapeutic potential and feasibility of targeting AKTIP for intervention or drug development.

Is AKTIP involved in any signaling pathways other than AKT?

AKTIP primarily interacts with and regulates AKT signaling. However, some studies suggest that AKTIP may also interact with other signaling molecules and pathways. For instance, AKTIP has been found to interact with phosphoinositide 3-kinase (PI3K) and contribute to PI3K-dependent signaling. Additionally, AKTIP has been reported to interact with Src kinase and play a role in Src-mediated signaling. Further investigation is needed to determine the extent of AKTIP's involvement in other signaling pathways.

Is AKTIP protein expressed in all tissues?

The expression of AKTIP protein is not well-documented in all tissues. However, studies have reported its expression in various tissues, including the heart, brain, liver, kidney, muscle, and immune cells. Different tissues may have different expression levels of AKTIP, and its expression may be regulated in a tissue-specific manner.

What are the known interactions of AKTIP protein?

AKTIP interacts with several proteins involved in AKT signaling and other cellular processes. Some of the known interactions include binding to AKT isoforms (AKT1, AKT2, AKT3) and modulating their activity and localization. AKTIP also interacts with other signaling molecules such as PI3K (phosphoinositide 3-kinase) and PHLPP (PH domain and leucine-rich repeat protein phosphatase), which regulate AKT activity.

Is there any disease association linked to AKTIP protein?

There is limited available information on disease associations specifically linked to AKTIP protein. However, dysregulation of AKT signaling has been implicated in various diseases, such as cancer, diabetes, and neurodegenerative disorders. Since AKTIP is involved in the regulation of AKT signaling, further research is needed to explore if any abnormalities or mutations in AKTIP are associated with specific diseases.

Are there any known post-translational modifications of AKTIP protein?

Current knowledge about post-translational modifications of AKTIP protein is limited. However, like many other proteins, it is possible that AKTIP undergoes post-translational modifications such as phosphorylation, acetylation, ubiquitination, or methylation. These modifications can potentially regulate AKTIP's function and interaction with other proteins, but further research is needed to fully understand the post-translational modifications of AKTIP.

Have there been any studies on the regulation of AKTIP expression?

Limited studies have investigated the regulation of AKTIP expression. One study found that the transcription factor EGR1 can bind to the promoter region of AKTIP and regulate its expression in certain cancer cells. Another study suggested a role for the microRNA miR-29a in downregulating AKTIP expression in ovarian cancer cells. More research is necessary to fully understand the mechanisms and factors involved in the regulation of AKTIP expression.

Are there any known diseases or disorders associated with AKTIP protein?

Currently, there are no specific diseases or disorders that have been directly linked to AKTIP protein. However, dysregulation of AKT signaling has been implicated in various diseases, including cancer, cardiovascular diseases, neurodegenerative diseases, and metabolic disorders. Since AKTIP interacts with AKT and regulates its activity, it is possible that alterations in AKTIP expression or function could indirectly contribute to the development or progression of these diseases. Further research is needed to explore any potential disease associations with AKTIP.

Are there any known functional roles of AKTIP protein beyond AKT signaling?

The primary known functional role of AKTIP protein is its interaction with and regulation of AKT signaling. However, there is evidence suggesting that AKTIP might have additional functional roles. For example, studies have shown that AKTIP is involved in the regulation of cell migration, invasion, and apoptosis. Further research is needed to elucidate the precise mechanisms and additional functional roles of AKTIP.