Recombinant Human AIG1, His-tagged
Cat.No. : | AIG1-9506H |
Product Overview : | Recombinant Human AIG1 protein, fused to His-tag, was expressed in E.coli and purified by Ni-sepharose. |
Availability | September 20, 2024 |
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Source : | E.coli |
Species : | Human |
Tag : | His |
Protein length : | 1-238a.a. |
Storage : | The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles. |
Storage Buffer : | 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 300mM Imidazole and 0.7% Sarcosyl, 15%glycerol. |
Gene Name : | AIG1 androgen-induced 1 [ Homo sapiens ] |
Official Symbol : | AIG1 |
Synonyms : | AIG1; androgen-induced 1; androgen-induced gene 1 protein; AIG 1; dJ95L4.1; FLJ10485; AIG-1; RP1-95L4.1; DKFZp686F03136; |
Gene ID : | 51390 |
mRNA Refseq : | NM_016108 |
Protein Refseq : | NP_057192 |
MIM : | 608514 |
UniProt ID : | Q9NVV5 |
Chromosome Location : | 6q24.1 |
Function : | protein binding; |
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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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Customer Reviews (4)
Write a reviewTheir timely and dependable assistance ensures a streamlined workflow, promoting efficient troubleshooting and data interpretation.
Its superior purity, reliability, and consistency make it an ideal choice to advance my research and attain accurate and precise results.
Their expert guidance and problem-solving approach effectively address any challenges or queries that may arise during my experimentation.
The AIG1 protein offers an exceptional level of quality that perfectly aligns with my experimental requirements.
Q&As (14)
Ask a questionThere is currently no known disease or disorder that is specifically associated with mutations in the AIG1 gene or alterations in AIG1 protein expression or function. However, further research is needed to fully understand the role of AIG1 in health and disease.
Yes, AIG1 protein has been shown to interact with several other proteins, including inositol 1,4,5-trisphosphate receptors and the mitochondrial protein LRPPRC, among others.
There is currently no direct evidence linking AIG1 protein to cancer. However, some studies have suggested that alterations in lipid metabolism and the formation of lipid droplets may be involved in the development and progression of certain cancers. Further research is needed to fully understand the potential role of AIG1 in cancer biology.
There is currently no known disease or disorder that is specifically associated with mutations in the AIG1 gene or alterations in AIG1 protein expression or function.
Various techniques are used to study AIG1 protein, including biochemical assays, cell culture and imaging techniques, and genetic manipulation of cells and organisms.
There are currently no known inhibitors or activators of AIG1 protein.
As of now, there are no known specific inhibitors or activators of AIG1 protein. However, further research may identify potential compounds or interventions that modulate AIG1 function.
There is currently no evidence supporting the use of AIG1 protein as a diagnostic or prognostic marker for any disease or disorder. However, further research may identify potential clinical applications for this protein in certain contexts.
As of now, there are no known drugs that specifically regulate AIG1 protein. However, further research may identify potential targets or compounds that modulate AIG1 function, particularly in the context of lipid metabolism or cellular stress response.
AIG1 protein is expressed in a variety of tissues, including the liver, kidney, brain, and heart, among others.
Yes, there are ongoing research studies on AIG1 protein. Some studies are aimed at understanding the molecular mechanisms underlying AIG1 function and regulation, while others are focused on elucidating the role of AIG1 in various cellular processes and disease states. Additionally, some research studies are aimed at developing new drugs or therapeutic strategies that target AIG1 or related pathways.
Although there is currently no known disease or disorder specifically associated with mutations in the AIG1 gene or alterations in AIG1 protein expression or function, further research may identify potential clinical significance for this protein.
AIG1 protein has been shown to play a role in the regulation of autophagy, a cellular process involved in the degradation and recycling of damaged or unwanted components. Specifically, AIG1 has been implicated in the formation of autolysosomes, which are organelles that contain cellular material targeted for degradation.
Currently, there are no known therapeutic applications of targeting AIG1 protein. However, further research may identify potential therapeutic strategies that target AIG1 or related pathways, particularly in the context of metabolic disorders or other diseases associated with lipid metabolism or cellular stress response.
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