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Recombinant Rhesus monkey ANKIB1 Protein, His-tagged

Cat.No. : ANKIB1-326R
Product Overview : Recombinant Rhesus monkey ANKIB1 full length or partial length protein was expressed.
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Source : Mammalian Cells
Species : Rhesus monkey
Tag : His
Form : Liquid or lyophilized powder
Endotoxin : < 1.0 EU per μg of the protein as determined by the LAL method.
Purity : >80%
Notes : This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.
Storage : Store it at +4 ºC for short term. For long term storage, store it at -20 ºC~-80 ºC.
Storage Buffer : PBS buffer
Gene Name : ANKIB1 ankyrin repeat and IBR domain containing 1 [ Macaca mulatta (Rhesus monkey) ]
Official Symbol : ANKIB1
Synonyms : ANKIB1; ankyrin repeat and IBR domain-containing protein 1;
Gene ID : 703273
mRNA Refseq : NM_001257769
Protein Refseq : NP_001244698
MIM :
UniProt ID : F7BY13

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (12)

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Are there any known post-translational modifications of ANKIB1 protein? 03/09/2022

Currently, there is limited information available regarding the post-translational modifications of ANKIB1 protein. However, like many other proteins, it is possible that ANKIB1 may undergo modifications such as phosphorylation, ubiquitination, or acetylation, which can regulate its stability, activity, or cellular localization. Further studies are needed to elucidate the post-translational modifications of ANKIB1 protein.

Are there any known functional domains or motifs in ANKIB1 protein? 01/08/2022

ANKIB1 protein contains multiple ankyrin repeat domains, which are known to mediate protein-protein interactions. Ankyrin repeat domains consist of approximately 33 amino acids and are characterized by a series of repeated structural units that form a helical hairpin structure. These domains are often involved in binding to specific protein partners. The presence of ankyrin repeat domains in ANKIB1 suggests its potential role in protein interactions and signaling.

Is ANKIB1 protein associated with any diseases or disorders? 02/06/2021

ANKIB1 has been found to be mutated in a small number of individuals with neurodevelopmental disorders, including intellectual disability and autism spectrum disorder. These findings suggest a potential role for ANKIB1 in normal brain development and function. Further research is needed to fully understand the involvement of ANKIB1 in disease processes.

Is ANKIB1 protein implicated in any human diseases? 10/12/2020

Mutations in the ANKIB1 gene have been associated with neurodevelopmental disorders, including intellectual disability and autism spectrum disorders. However, these mutations are rare, and more research is needed to establish a clear link between ANKIB1 protein and these diseases.

Are there any known interactors or binding partners of ANKIB1 protein? 08/28/2019

The specific binding partners or interactors of ANKIB1 protein have not been extensively characterized yet. Further research is required to investigate its protein-protein interactions and identify potential binding partners.

Are there any known orthologs of ANKIB1 protein? 03/28/2019

Yes, ANKIB1 has orthologs in various species. For example, in mice, the ANKIB1 protein is referred to as Ankib1. Orthologs of ANKIB1 can be found by conducting comparative genomics analyses across different species. These orthologous proteins may provide insights into the evolutionary conservation and functional roles of ANKIB1.

Is ANKIB1 protein involved in any signaling pathways? 03/09/2019

its potential role in protein-protein interactions suggests that it may participate in signaling cascades by interacting with other signaling molecules. Further research is necessary to uncover the exact signaling pathways in which ANKIB1 protein is involved.

Are there any known functional domains or motifs in ANKIB1 protein? 08/01/2018

ANKIB1 protein contains ankyrin repeat domains, which are common protein-protein interaction motifs found in many proteins involved in diverse cellular processes. It also possesses an IBR domain, which suggests potential involvement in protein stability and ubiquitin ligase activity.

Are there any interacting partners or binding partners of ANKIB1 protein? 03/16/2018

The specific interacting partners or binding partners of ANKIB1 protein have not been extensively studied. However, as ankyrin repeat domains are known to mediate protein-protein interactions, it is possible that ANKIB1 may interact with other proteins in the cell. Future research may help identify the specific binding partners and elucidate the functional implications of these interactions.

Is ANKIB1 protein tissue-specific? 07/04/2017

ANKIB1 protein is broadly expressed in various tissues, including the brain, heart, liver, and skeletal muscles.

What are the potential functions of ANKIB1 protein? 11/06/2016

Although the exact functions of ANKIB1 protein are still not fully understood, its ankyrin repeat domains suggest a potential role in protein-protein interactions and regulation of cellular processes. Additionally, the presence of the IBR domain suggests a possible involvement in protein stability and ubiquitin ligase activity. However, further research is needed to determine its precise functions.

What are the diseases associated with ANKIB1 protein mutations? 11/05/2016

Mutations in the ANKIB1 gene have been identified in a very limited number of cases with neurodevelopmental disorders such as intellectual disability and autism spectrum disorders. However, more research is needed to establish a clear association between ANKIB1 mutations and these conditions.

Customer Reviews (4)

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Reviews
11/18/2022

    This protein exhibits outstanding performance in ELISA, providing accurate and reliable results in detecting and quantifying specific antigens.

    01/12/2020

      Its high sensitivity ensures the detection of even low abundance targets, making it a valuable tool in immunoassays.

      01/07/2020

        Its stability and compatibility with electron microscopy techniques make it an excellent choice for studying protein structures at high resolution.

        11/19/2016

          Its versatility in various biological applications, along with its compatibility with different techniques, strongly recommend it as a preferred reagent for researchers in the field.

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