Recombinant Human VDAC1/Porin Protein

Beta LifeScience SKU/CAT #: BLA-9612P

Recombinant Human VDAC1/Porin Protein

Beta LifeScience SKU/CAT #: BLA-9612P
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Product Overview

Host Species Human
Accession P21796
Synonym N2441 OMP2 POR1 hVDAC1 MGC111064 Mitochondrial Porin Outer mitochondrial membrane protein porin 1 Plasmalemmal porin Porin 31HL Porin 31HM VDAC VDAC-1 Vdac1 VDAC1_HUMAN Voltage dependent anion channel 1 Voltage dependent anion selective channel protein 1 Voltage-dependent anion-selective channel protein 1 YNL055C YNL2441C
Description Recombinant Human VDAC1/Porin Protein was expressed in Wheat germ. It is a Full length protein
Source Wheat germ
AA Sequence MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTE TTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFD SSFSPNTGKKNAKIKTGYKREHINLGCDMDFDIAGPSIRGALVLGYEGWL AGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNK KLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQT LKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA
Molecular Weight 57 kDa including tags
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol. In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. May mediate ATP export from cells.
Subcellular Location Mitochondrion outer membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Membrane raft; Multi-pass membrane protein.
Protein Families Eukaryotic mitochondrial porin family
Database References
Tissue Specificity Expressed in erythrocytes (at protein level). Expressed in heart, liver and skeletal muscle.

Gene Functions References

  1. VDAC1 allows Ca(2+) access to the MCU, facilitating transport of Ca(2+) to the matrix, and also from the IMS to the cytosol. Intra-mitochondrial Ca(2+) controls energy production and metabolism by modulating critical enzymes in the tricarboxylic acid (TCA) cycle and fatty acid oxidation. PMID: 29594867
  2. associate dysfunction in Fe-S cluster biogenesis with cleavage of VDAC1 PMID: 29596470
  3. HK1 competes with SOD1 G93A mutant from familial amyotrophic lateral sclerosis cases for binding VDAC1.SOD1 G93A mutant from familial amyotrophic lateral sclerosis cases binds VDAC1 with high affinity. PMID: 27721436
  4. Study shows that silencing voltage-dependent anion channel 1 (VDAC1) expression using short interfering RNA-VDAC1 in 9 glioblastoma-related cell lines, including patient-derived cells, led to marked decreases in VDAC1 levels and cell growth. PMID: 28339833
  5. VDAC1 plays an important role in dengue virus infection. PMID: 27779201
  6. VDAC1 is a direct target of miR-320a in non-small cell lung cancer (NSCLC) cells, and miR-320a inhibits VDAC1 expression in NSCLC cells PMID: 27304056
  7. The results of this study shown VDAC1, the Potential Target of miR-320a, is Upregulated in Response to HIV-1 Tat. PMID: 27761954
  8. the present study indicated that VDAC1 may interact with HPV16 E7 to promote the malignant progression of HPV-related cervical cancer PMID: 27419626
  9. Porin expression was lower in patients with heart failure with preserved ejection fraction compared to controls. PMID: 27179829
  10. Studied voltage-dependent anion channel 1 (VDAC1) structure and oligomerization using an Escherichia coli cell-free protein synthesis system and bicelle crystallization. PMID: 28608415
  11. In this study, molecular dynamics simulations and single-channel experiments of VDAC-1 show agreement for the current-voltage relationships of an "open" channel and they also show several subconducting transient states that are more cation selective in the simulations. We observed voltage-dependent asymmetric distortions of the VDAC-1 barrel and the displacement of particular charged amino acids. PMID: 27653481
  12. VDAC1 was accumulated in the desmin highly stained area of muscle fibers of desminopathy patients. PMID: 27941998
  13. work raises the interesting possibility that cholesterol-mediated regulation of VDAC1 may be facilitated through a specific binding site at the functionally important Glu(73) residue. PMID: 28396346
  14. this study describes novel drug candidates with a defined mechanism of action that involves inhibition of VDAC1 oligomerization, apoptosis, and mitochondrial dysfunction. The compounds VBIT-3 and VBIT-4 offer a therapeutic strategy for treating different diseases associated with enhanced apoptosis and point to VDAC1 as a promising target for therapeutic intervention. PMID: 27738100
  15. Results from the simulations show that HK2 binding restricts the movement of the VDAC1 N-terminal helix. As a result, VDAC1 is kept in the open state most of the time and probably allows a constant supply of ATP to HK2 for glycolysis. PMID: 27544294
  16. The findings of this study suggest that inhibition of intracellular Ca(2+/-) overload could protect cells from damage and that VDAC1 plays a considerable role in Cr(VI)-induced liver injury. PMID: 27898307
  17. Our study suggested that miR-7 suppressed the expression of VDAC1 in hepatocellular carcinoma PMID: 26831666
  18. Results shows that beta-barrel of human VDAC1 embedded into a membrane is highly flexible and that Ca2+, a key regulator of metabolism and apoptosis, strongly decreases its plasticity suggesting that physiological VDAC function depends on the molecular plasticity of its channel. PMID: 27021164
  19. High VDAC1 expression is associated with cervical cancer. PMID: 26716410
  20. Studies using B16F10 and A375 cells genetically modified for ATF2 indicated that mitochondrial ATF2 was able to dissociate Bim from the Mcl-1/Bim complex to trigger VDAC1 oligomerization. PMID: 26462148
  21. findings also suggest that VDAC1 may be a novel biomarker for gastric cancer PMID: 26646027
  22. serum starvation induces CREB1 expression, in turn activating miR-320a expression, which then down-regulates VDAC1 expression to facilitate mitophagy PMID: 26472185
  23. Reducing VDAC1 expression induces a non-apoptotic role for pro-apoptotic proteins in glioblastoma multiforme cancer cell differentiation. PMID: 27080741
  24. The works available on VDAC cysteines support the notion that VDAC1, VDAC2, and VDAC3 proteins are paralogs with a similar pore-function and slightly different, but important, ancillary biological functions. (Review) PMID: 26947058
  25. The protective effect of miR-7 is partly exerted through promoting mitochondrial function by targeting VDAC1 expression. PMID: 26801612
  26. Data show that voltage-dependent anion channel 1 (VDAC1) knockout cells are resistant to AMP-activated protein kinase (AMPK) and mechanistic target of rapamycin (mTOR) modulation by itraconazole, indicating VDAC1 is the mediator of the activity. PMID: 26655341
  27. Amyloid beta -mediated toxicity involves mitochondrial and plasma membrane VDAC1, leading to mitochondrial dysfunction and apoptosis induction. PMID: 26542804
  28. PGC-1alpha deficiency exacerbates high glucose-induced apoptosis in human umbilical vein endothelial cells through activation of VADC1. PMID: 26191154
  29. The serum lever of Alzheimer's disease were increase and the expression of VDAC1 strongly correlated with the Mini-Mental State Examination scores of the AD patients. PMID: 25502766
  30. VDAC1 is involved in the process of mitochondria-mediated apoptosis by mediating the release of apoptotic proteins and interacting with anti-apoptotic proteins. (Review) PMID: 25448878
  31. The functional interactions between VDAC and alpha-syn, revealed by the present study, point toward the long sought after physiological and pathophysiological roles for monomeric alpha-syn in PD and in other alpha-synucleinopathies PMID: 26055708
  32. Results show that BNIP3 interacts with the voltage-dependent anion channel (VDAC) to directly induce mitochondrial release and nuclear translocation of EndoG. PMID: 25436615
  33. TP53 regulation of VDAC1 cleavage occurs through mitochondrial Mieap and is dependent on the endolysosomal pH. PMID: 25691661
  34. These data suggest that an interaction between Mcl-1 and VDAC promotes lung cancer cell migration by a mechanism that involves Ca(2+)-dependent reactive oxygen species production. PMID: 25341036
  35. data indicate that the BH4 domain of Bcl-XL, but not that of Bcl-2, selectively targets VDAC1 and inhibits apoptosis by decreasing VDAC1-mediated Ca(2+) uptake into the mitochondria PMID: 25681439
  36. Voltage-dependent structural changes of hVDAC1 PMID: 24728177
  37. VDAC1 was expressed and reconstituted into two-dimensional lipid crystalline bilayers with characteristics identical to wild type samples. PMID: 25545271
  38. Results indicate that mitochondrial function associated with VDAC1 is decreased in sporadic and experimental Parkinson's disease, and this decrease is associated with alpha-synuclein accumulation and aggregation PMID: 24825319
  39. Data indicate that voltage-dependent anion channel 1 (VDAC1) is involved in plasminogen kringle 5 (K5)-induced activation of the mitochondrial apoptosis pathway. PMID: 25296756
  40. Data indicate that curcumin interacts with residues in the alpha helical N-terminus of voltage dependent anion channel VDAC-1 and in the channel wall. PMID: 25459681
  41. Ca(2+)-mediated regulation of VDAC1 expression levels is associated with cell death induction. PMID: 24704533
  42. Label-free quantitative comparison of DN urinary exosomes vs control group and SRM further validation, resulted in the discovery of a panel of three proteins (AMBP, MLL3 and VDAC1) which changes in DN. PMID: 24211404
  43. the C-terminus end of VDAC faces the mitochondrial inter-membrane space. PMID: 24324700
  44. This review examines the significance of this new form of VDAC1 for anticancer therapy.[review] PMID: 24272356
  45. Nucleotide interactions of the human voltage-dependent anion channel. PMID: 24668813
  46. Increase in mRNA levels of the voltage-dependent anion channel 1 gene is associated with Alzheimer's disease. PMID: 24063855
  47. Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease. PMID: 22926141
  48. VDAC binds tissue-type plasminogen activator (t-PA) on human neuroblastoma SK-N-SH cells PMID: 23161549
  49. VDAC 1, 2, and 3 recruit Parkin to defective mitochondria to promote mitochondrial autophagy. PMID: 23060438
  50. The N-terminal helix of VDAC1 controls entry into elliptic beta-barrel states which underlie VDAC closure. PMID: 22841291

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.

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