Recombinant Human Beclin 1-Associated Autophagy-Related Key Regulator (ATG14) Protein (His&Myc)

Name: Recombinant Human Beclin 1-Associated Autophagy-Related Key Regulator (ATG14) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-02499P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATG14.

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Product Overview

Description	Recombinant Human Beclin 1-Associated Autophagy-Related Key Regulator (ATG14) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q6ZNE5
Target Symbol	ATG14
Synonyms	4832427M01; ATG14; Atg14L; Autophagy-related protein 14-like protein; BAKOR_HUMAN; Barkor; Beclin 1-associated autophagy-related key regulator; D14Ertd114e; D14Ertd436e; KIAA0831; mCG_6911
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRIEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNPAYTISAALCYATQLVNILSHILDVNLPKKLCNSEFCGENLSKQKFTRAVKKLNANILYLCFSQHVNLDQLQPLHTLRNLMYLVSPSSEHLGRSGPFEVRADLEESMEFVDPGVAGESDESGDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR
Expression Range	1-492aa
Protein Length	Full Length
Mol. Weight	60.3kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1. Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK. Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion. Modulates the hepatic lipid metabolism.
Subcellular Location	Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein. Preautophagosomal structure membrane; Peripheral membrane protein. Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein.
Protein Families	ATG14 family
Database References	HGNC: 19962 OMIM: 613515 KEGG: hsa:22863 STRING: 9606.ENSP00000247178 UniGene: PMID: 30121664 This study identifies an unexpected role for PtdIns(4,5)P2 signaling in the regulation of ATG14 complex and autophagy. PMID: 27621469 These data provide evidence for additional roles of Atg2A and Atg14L in the formation of early autophagosomal membranes and also in lipid metabolism. PMID: 24776541 we found that ATG14 interacted with Ulk1 and LC3, and knock down of Ulk1 prevented the lipidation of LC3 and autophagy in HeLa-ATG14 cells. We also identified a phosphatidylethanolamine (PE) binding region in ATG14, and the addition of Ulk1 to Hela-ATG14 cells decreased the ATG14-PE interaction. PMID: 28069524 polar BECN2 CCD interface residues result in a metastable homodimer, facilitating dissociation, but enable better interactions with polar ATG14 residues stabilizing the BECN2:ATG14 heterodimer. PMID: 28218432 use circular dichroism and small-angle X-ray scattering (SAXS) to show that the ATG14 coiled-coil domain (CCD) is significantly disordered but becomes more helical in the BECN1:ATG14 heterodimer, although it is less well-folded than the BECN1 CCD homodimer PMID: 27383850 These results define a key molecular event for the starvation-induced activation of the ATG14-containing PtdIns3K complex by ULK1. PMID: 27046250 data suggest an autophagy-specific membrane fusion mechanism in which oligomeric ATG14 directly binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion PMID: 25686604 Cisplatin upregulated Barkor protein levels of the Saos-2 cell line. PMID: 24337183 Atg14 is critical in controlling an autophagy-dependent phosphorylation of beclin-1. We map novel phosphorylation sites to serines 90 and 93 and demonstrate that phosphorylation at these sites is necessary for maximal autophagy. PMID: 23878393 Our findings reveal that Atg14L, previously considered to be solely a Beclin 1-binding autophagy protein, plays a novel role in the late stage of endocytic trafficking in conjunction with Snapin PMID: 22797916 Anaplasma actively induces autophagy by secreting Ats-1 that hijacks the Beclin 1-Atg14L autophagy initiation pathway likely to acquire host nutrients for its growth PMID: 23197835 Atg14 is a new target gene of FoxOs and the core clock machinery, and this gene plays an important role in hepatic lipid metabolism PMID: 22992773 analysis of how the Beclin1 coiled-coil domain interface regulates homodimer and heterodimer formation with Atg14L and UVRAG PMID: 22314358 Data suggest that the Atg14L-dependent appearance of phosphatidylinositol 3-phosphate in the endoplasmic reticulum makes this organelle the platform for autophagosome formation. PMID: 20713597 These results suggest that mammalian cells have at least two distinct class III PI3-kinase complexes, and that beclin 1 interacts distinctly with mammalian Atg14 and UVRAG in two of these complexes. PMID: 18843052 study defines a regulatory signaling pathway mediated by Barkor (KIAA0831) that positively controls autophagy through Beclin 1 PMID: 19050071 Two Beclin 1 associated proteins, Atg14L and Rubicon, were identified. PMID: 19270696 Barkor/KIAA0831 functions as an autophagy targeting factor for Beclin 1 and the class III PI3 kinase. Barkor and UVRAG form two distinct protein complexes with the core class III PI3 kinase. Barkor is a functional ortholog of yeast Atg14. PMID: 19050071

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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.