Recombinant Human ATG3 Protein

Name: Recombinant Human ATG3 Protein
Brand: Beta LifeScience
SKU: BL-2051NP
Availability: InStock

BL-2051NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Ubiquitin-like-conjugating Enzyme ATG3/ATG3 is produced by our E.coli expression system and the target gene encoding Met1-Met314 is expressed.
Accession	Q9NT62
Synonym	Ubiquitin-like-conjugating enzyme ATG3; Autophagy-related protein 3; APG3-like; hApg3; Protein PC3-96; ATG3; APG3; APG3L
Gene Background	Ubiquitin-like-conjugating enzyme ATG3 (ATG3), also known as Apg3L and Apg3p, functions as a regulatory component of autophagosome biogenesis necessary for autophagy. ATG3 exhibits 98% aa sequence identity with both its mouse and rat orthologs. It is widely expressed and has highly levels in heart, skeletal muscle, kidney, liver and placenta. As an E2-like enzyme, involves in autophagy and mitochondrial homeostasis. ATG3 catalyzes the conjugation of ATG8-like proteins to PE which is essential for autophagy. ATG3 also can catalyze the conjugation of ATG12 to itself which palys a role in mitochondrial homeostasis but not in autophagy.
Molecular Mass	36 KDa
Apmol Mass	38 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 10% Glycerol, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.
Subcellular Location	Cytoplasm.
Protein Families	ATG3 family
Database References	HGNC: 20962 OMIM: 609606 KEGG: hsa:64422 STRING: 9606.ENSP00000283290 UniGene: Hs.477126
Tissue Specificity	Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta.

Gene Functions References

ATG3 was targeted by miR-23a, suggesting that ATG3 is an autophagy-related competing endogenous RNA. PMID: 30007957
Results revealed that miR-16 was significantly downregulated, and ATG3 was significantly upregulated in non-small cell lung carcinoma (NSCLC) patient tissue samples. ATG3 was found to be a direct target of miR-16. PMID: 29138833
miR-155 silencing rescued autophagosome number in Mycobacterium tuberculosis infected dendritic cells and enhanced autolysosome fusion, thereby supporting a previously unidentified role of the miR-155 as inhibitor of ATG3 expression. PMID: 29300789
PTK2 inhibition-induced sustained levels of ATG3 were able to sensitize cancer cells to DNA-damaging agents. PMID: 28103122
Our data demonstrate that HOTAIR promotes the activation of autophagy in HCC cells by upregulating the expression of the autophagy-related genes ATG3 and ATG7. PMID: 27301338
ATG3 upregulation contributes to autophagy induced by the detachment of intestinal epithelial cells from the extracellular matrix, but promotes autophagy-independent apoptosis of the attached cells PMID: 26061804
Hidden Markov models were used to detect protein homology among the flexible regions of Atg3 homologs and importance of conserved regions evaluated by performing affinity capture experiments with human Atg3 deletion constructs; binding studies and competition experiments demonstrate that overlapping sites in the Atg3FR are important for E3 binding and E1 binding. PMID: 24186333
The region of human ATG3 that interacts with ATG7 is precisely identified using nuclear magnetic resonance. PMID: 26043688
ATG3 gene and its gene family may play an important role in transformation of myelodysplastic syndrome. PMID: 24420857
Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3. PMID: 24747438
13 residues of the ATG3 fragment form a short beta-strand followed by an alpha-helix on a surface area that is an exclusive binding site for ATG12. PMID: 24191030
caspase-8 overexpression led to Atg3 degradation and this event depended on caspase-8 enzymatic activity PMID: 22644571
These results unveil a role for ATG12-ATG3 in mitochondrial homeostasis and implicate the ATG12 conjugation system in cellular functions distinct from the early steps of autophagosome formation. PMID: 20723759
Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p PMID: 11825910
Murine Atg8L/Apg8L modification is mediated by human Atg3. PMID: 16704426

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.