Recombinant Human ADIG 293 Cell Lysate

• Cat.No.: ADIG-9010HCL

Specification

• Description: Antigen standard for adipogenin (ADIG) is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid and then lysed in RIPA Buffer. Protein concentration was determined using a colorimetric assay. The antigen control carries a C-terminal Myc/DDK tag for detection.
• Source: HEK 293 cells
• Species: Human
• Components: This product includes 3 vials: 1 vial of gene-specific cell lysate, 1 vial of control vector cell lysate, and 1 vial of loading buffer. Each lysate vial contains 0.1 mg lysate in 0.1 ml (1 mg/ml) of RIPA Buffer (50 mM Tris-HCl pH7.5, 250 mM NaCl, 5 mM EDTA, 50 mM NaF, 1% NP40). The loading buffer vial contains 0.5 ml 2X SDS Loading Buffer (125 mM Tris-Cl, pH6.8, 10% glycerol, 4% SDS, 0.002% Bromophenol blue, 5% beta-mercaptoethanol).
• Size: 0.1 mg
• Storage Instruction: Store at -80°C. Minimize freeze-thaw cycles. After addition of 2X SDS Loading Buffer, the lysates can be stored at -20°C. Product is guaranteed 6 months from the date of shipment.
• Applications: ELISA, WB, IP. WB: Mix equal volume of lysates with 2X SDS Loading Buffer. Boil the mixture for 10 min before loading (for membrane protein lysates, incubate the mixture at room temperature for 30 min). Load 5 ug lysate per lane.

Gene Information

• Gene Name: ADIG adipogenin [ Homo sapiens ]
• Official Symbol: ADIG
• Synonyms: adipogenin; SMAF1; adipogenesis associated; MGC39724; RP5-1100H13.2; small adipocyte factor 1 (SMAF1)
• Gene ID: 149685
• mRNA Refseq: NM_001018082.1
• Protein Refseq: NP_001018092.1
• MIM: 611396
• UniProt ID: Q0VDE8
• Chromosome Location: 20q11.23

Q&As

Is there any evidence that ADIG proteins are involved in embryonic development?

There is limited evidence to suggest that ADIG proteins may play a role in embryonic development. For example, ADIG expression has been shown to be regulated by the retinoic acid signaling pathway, which plays a critical role in embryonic development. In zebrafish, knockdown of ADIG homologs has been shown to affect gastrulation and patterning of the embryonic axis. However, the specific role of ADIG proteins in embryonic development requires further study.

Do ADIG proteins have any known interactions with other proteins?

Yes, ADIG proteins have been shown to interact with a variety of other proteins. For example, ADIG interacts with ARF GAPs and regulates vesicle trafficking. AIG1 interacts with huntingtin and has been implicated in the pathogenesis of Huntington's disease. AIG2 interacts with mTOR and regulates cell growth. In addition, ADIG has been shown to interact with several other proteins involved in cancer and signal transduction pathways, such as phospholipase C-gamma, integrin-linked kinase, and protein kinase C-epsilon.

Are there any known interacting partners of ADIG proteins?

Yes, ADIG proteins have been shown to interact with a variety of other proteins in different cellular processes. For example, ADIG has been shown to interact with the oncogenic protein c-Myc and the tumor suppressor protein p53 in cancer cells. AIG1 has been shown to interact with the huntingtin protein, which is mutated in Huntington's disease, and with Pex19, a protein involved in peroxisome biogenesis. ADIG proteins have also been shown to interact with multiple proteins involved in vesicle trafficking, such as Sec23/24 and COPII. These interactions suggest that ADIG proteins may play important roles in cellular signaling, protein trafficking, and protein function.

Are there any drugs or therapies targeting ADIG proteins?

There are currently no drugs or therapies targeting ADIG proteins. However, understanding the role of ADIG proteins in disease could lead to the development of new therapies for cancer and neurodegenerative diseases. In addition, small molecules that target ARF GTPases, which are regulated by ADIG proteins, have shown potential as therapeutic agents. Future studies may explore the therapeutic potential of targeting ADIG proteins directly or indirectly.

Are there any diseases or disorders associated with ADIG proteins?

There is currently limited information on the role of ADIG proteins in disease. However, some studies have suggested that ADIG proteins may play a role in cancer and neurodegenerative diseases. For example, ADIG has been shown to interact with several proteins involved in cancer, and overexpression of ADIG has been observed in some cancer cell lines. AIG1 has also been implicated in the pathogenesis of Huntington's disease, and mutations in the AIG1 gene have been identified in patients with the disease. Further research is needed to fully understand the role of ADIG proteins in disease.

How are ADIG proteins regulated?

The regulation of ADIG proteins is not well understood, but some studies suggest that post-translational modifications such as phosphorylation and ubiquitination may play a role in their regulation. For example, phosphorylation of ADIG by protein kinase C (PKC) has been shown to increase its GTPase-activating activity. In addition, a ubiquitin ligase called Cbl-b has been shown to interact with ADIG and regulate its stability.

Are there any inhibitors or activators of ADIG proteins?

There are currently no known inhibitors or activators of ADIG proteins, although some studies have suggested that phosphorylation and ubiquitination may play a role in their regulation. In addition, several small molecules have been identified that can interact with ARF GTPases and modulate their activity, and it is possible that these compounds could also affect the activity of ADIG proteins.

How are ADIG proteins involved in vesicle trafficking?

ADIG proteins are involved in vesicle trafficking by regulating the activity of ARF GTPases. ARF GTPases are involved in the formation and transport of vesicles between different cellular compartments, and ADIG proteins have been shown to interact with ARF GAPs and regulate their activity. By regulating ARF-mediated vesicle trafficking, ADIG proteins may play a role in the secretion of hormones and neurotransmitters, the formation of the Golgi apparatus, and the regulation of membrane trafficking in general.