AKAP1B
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Zebrafish | AKAP1B-5652Z | Recombinant Zebrafish AKAP1B | Mammalian Cell | His |
- Involved Pathway
- Protein Function
- Interacting Protein
AKAP1B involved in several pathways and played different roles in them. We selected most pathways AKAP1B participated on our site, such as Factors involved in megakaryocyte development and platelet production, G Protein Signaling Pathways, Hemostasis, which may be useful for your reference. Also, other proteins which involved in the same pathway with AKAP1B were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
---|---|
Factors involved in megakaryocyte development and platelet production | IRF1B;HBB-BH1;AKAP1;MAFG;KIF26A;NFE2;KIF5A;MFN2;KDM1A |
G Protein Signaling Pathways | AKAP8;GNB3B;AKAP12;GNB5B;KCNJ3;AKAP10;Akap3;GNA13;AKAP6 |
Hemostasis | ANGPT2A;KIF5A;IGF2B;SLC16A8;CEACAM6;SERPINF2B;SLC8A2A;GNA13B;MMRN2A |
AKAP1B has several biochemical functions, for example, RNA binding, nucleic acid binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AKAP1B itself. We selected most functions AKAP1B had, and list some proteins which have the same functions with AKAP1B. You can find most of the proteins on our site.
Function | Related Protein |
---|---|
RNA binding | CTIF;KHDC3;A1CF;NSUN3;NCL;PCBP3;CWC22;RPL9;PRAC |
nucleic acid binding | DDX4;RNASE4;ZFP828;ZFPM2;PNLDC1;PRKRIRA;SALL3B;GTF2H2;TRIM27 |
AKAP1B has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AKAP1B here. Most of them are supplied by our site. Hope this information will be useful for your research of AKAP1B.
- Q&As
- Reviews
Q&As (15)
Ask a questionAs of now, there is limited information on the specific interacting partners of AKAP1B. However, AKAPs in general have been found to interact with various signaling molecules, including PKA, protein kinase C (PKC), and phosphatases. They can also bind to other scaffolding or adapter proteins, allowing for the assembly of signaling complexes. It is likely that AKAP1B interacts with similar molecules, but further research is needed to identify and characterize its specific binding partners.
As of now, there are no specific knockout or transgenic animal models reported for AKAP1B. However, animal models with altered expression or function of other AKAP family members, such as AKAP5 or AKAP7, have been used to study their roles in cellular and physiological processes. It is possible that similar animal models could be developed in the future to investigate the specific functions and roles of AKAP1B in vivo.
As an AKAP protein, AKAP1B is believed to play a role in cellular signaling pathways by organizing and targeting PKA and other signaling molecules. PKA is a key player in numerous signaling cascades, and its precise localization within the cell is critical for mediating specific downstream effects. AKAPs, including AKAP1B, help to direct the localization of PKA, allowing for efficient and precise signaling within cells.
Experimental methods to study AKAP1B include techniques such as immunofluorescence microscopy and subcellular fractionation to determine its cellular localization. Co-immunoprecipitation (Co-IP) and pull-down assays can be employed to identify and characterize interacting partners of AKAP1B. Gene silencing techniques, such as RNA interference (RNAi), can be used to study the functional effects of knocking down AKAP1B expression in cellular or animal models. Biochemical assays can also be performed to examine the binding and assembly of AKAP1B with PKA and other signaling molecules.
The presence of genetic alterations or mutations in AKAP1B has not been extensively studied. However, genetic variations, such as SNPs, can occur within AKAP genes. It is possible that similar genetic alterations or mutations can occur in AKAP1B, but further research is required to determine their prevalence and impact on protein function.
Yes, there are several other proteins that belong to the AKAP family. Some examples include AKAP1, AKAP2, AKAP3, AKAP4, AKAP5, AKAP6, AKAP7, and AKAP8. These proteins share similar structural features and functions as AKAP1B, acting as scaffold proteins to anchor PKA and other signaling molecules in specific cellular compartments.
The regulation of AKAP1B within cells is not fully understood, as research on this protein is limited. However, other AKAPs are regulated through various mechanisms. For example, AKAP5 is known to be regulated by phosphorylation, protein-protein interactions, and subcellular localization. It is likely that AKAP1B may be regulated in a similar manner, but further studies are needed to elucidate the specific mechanisms controlling its expression, localization, and function.
The exact contribution of AKAP1B to neuronal function and synaptic transmission is not yet fully understood. However, as AKAP1B is primarily expressed in the brain, particularly in regions associated with learning, memory, and cognition, it is likely to play a role in these processes. AKAPs, including AKAP1B, are involved in the organization of protein signaling complexes at specific subcellular locations, such as synapses, where they regulate the activity and localization of key signaling molecules.
AKAP1B is primarily expressed in the brain, particularly in regions associated with learning, memory, and cognition. However, limited information is available regarding its expression in other tissues. The AKAP1 gene, which gives rise to AKAP1B and other isoforms, is known to be expressed in various tissues, including the heart, lung, liver, and testis. It is possible that AKAP1B may also be present in low levels or have tissue-specific expression outside of the brain, but more research is needed to fully characterize its expression pattern in different tissues.
The specific protein interactions or binding partners of AKAP1B have not been extensively characterized. However, other members of the AKAP family interact with a variety of proteins to form specific signaling complexes.
AKAP1B is primarily known for its interaction with PKA, serving as a scaffold to anchor PKA to specific cellular locations. However, it is possible that AKAP1B may also interact with other signaling molecules or proteins, although these interactions have not been extensively studied. AKAPs in general have been found to interact with a range of signaling molecules, including protein kinases, phosphatases, and other kinases. Therefore, further investigation is needed to determine if AKAP1B has interactions beyond PKA and to identify its potential binding partners in cellular signaling pathways.
The therapeutic targeting of AKAP1B is currently a topic of ongoing research, and no specific drugs or therapies have been developed to target this particular isoform. However, targeting other members of the AKAP family has shown potential therapeutic benefits in certain conditions.
The potential therapeutic targeting of AKAP1B has not been extensively investigated, as its specific role and significance in cellular pathways are still not well understood. However, targeting AKAPs in general has shown promise for therapeutic interventions. For example, peptide-based inhibitors have been developed to disrupt the interaction between AKAPs and PKA, leading to altered signaling and potential therapeutic benefits. Further research focusing on the function and interactions of AKAP1B might reveal opportunities for therapeutic targeting.
Currently, there is limited information on the tissue-specific expression of AKAP1B. AKAPs in general have been found to be expressed in a variety of tissues and cell types, with some showing preferential expression in specific organs or cell populations. Further studies are needed to determine the precise expression pattern of AKAP1B.
The association between AKAP1B and neurological disorders has not yet been extensively studied. However, alterations in other AKAP isoforms have been implicated in certain neurological disorders. For example, mutations in AKAP9 have been identified in patients with intellectual disability, autism spectrum disorders, and schizophrenia.
Customer Reviews (3)
Write a reviewWith this protein in hand, I am confident that my experiments will yield accurate and reliable results, advancing my scientific endeavors.
Its exceptional purity and functionality make it an ideal candidate to fulfill the objectives of my research.
The AKAP1B protein stands as a pinnacle of excellence, offering unparalleled quality that perfectly aligns with my experimental requirements.
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