Recombinant Human Vesicle-Associated Membrane Protein-Associated Protein B/C (VAPB) Protein (His), Active

Name: Recombinant Human Vesicle-Associated Membrane Protein-Associated Protein B/C (VAPB) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05608P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Vesicle-Associated Membrane Protein-Associated Protein B/C (VAPB) Protein (His), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined by its ability to bind Human EphB2 in functional ELISA is less than 20 ug/ml.
Uniprotkb	O95292
Target Symbol	VAPB
Synonyms	VAPB; UNQ484/PRO983; Vesicle-associated membrane protein-associated protein B/C; VAMP-B/VAMP-C; VAMP-associated protein B/C; VAP-B/VAP-C
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Complete Sequence	AKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAKPEDLMDSKLRCVFELPAENDKP
Expression Range	2-132aa
Protein Length	Partial
Mol. Weight	16 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 1xPBS, pH 7.4
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	Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation.
Subcellular Location	Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Protein Families	VAMP-associated protein (VAP) (TC 9.B.17) family
Database References	HGNC: 12649 OMIM: 182980 KEGG: hsa:9217 STRING: 9606.ENSP00000417175 UniGene: PMID: 28993872 the component proteins of the machinery, OSBP, VAP, SAC1, and PITPNB, are all essential host factors for AiV replication. Importantly, the machinery is directly recruited to the RNA replication sites through previously unknown interactions of VAP/OSBP/SAC1 with the AiV proteins and with ACBD3. PMID: 29367253 Lifelong elevation of neuronal VAPB slowed the decline of neurological impairment, delayed denervation of hindlimb muscles, and prolonged survival of spinal motor neurons. PMID: 28173107 Study showed that alpha-synuclein perturbs endoplasmic reticulum-mitochondria associations and that this involves disruption to the VAPB-PTPIP51 tethering proteins. Using a range of assays including immunoprecipitation, cellular glutathione S-transferase pull-down, proximity ligation and in vitro binding of recombinant proteins, study showed that alpha-synuclein is a direct binding partner for VAPB. PMID: 28337542 ACBD5-VAPB interaction regulates peroxisome-endoplasmic reticulum associations. Loss of PO-ER association perturbs PO membrane expansion and increases PO movement. PMID: 28108524 VAP-ACBD5-mediated contact between the endoplasmic reticulum and peroxisomes mediate organelle maintenance and lipid homeostasis. PMID: 28108526 Effects of the combined absence of VAPA and VAPB in human cells were studied; cells lacking VAP accumulate high levels of PI4P, actin comets, and trans-Golgi proteins on endosomes. Such defects are mimicked by downregulation of OSBP, a VAP interactor and PI4P transporter that participates in VAP-dependent endoplasmic reticulum-endosomes tethers. PMID: 27419871 this is the first study to report Amyotrophic lateral sclerosis caused by a VAPB mutation in a Chinese population. PMID: 26566915 Our work revealed that VAP-A/B knockdown impaired the processing and secretion of PAUF, which is one of the cargo proteins of carriers of the trans-Golgi network to the cell surface. PMID: 26490117 Heterozygous P56S Vapb knock-in mice show mild age-dependent defects in motor behaviors as characteristic features of the disease. The homozygous P56S Vapb knock-in mice show more severe defects compared with heterozygous mice reflecting the dominant and dose-dependent effects of P56S mutation. PMID: 26362257 VAPB inhibited the degradation of DeltaF508-CFTR in the ER through interactions with the RMA1-Derlin-BAP31-VCP pathway. PMID: 26740627 Study characterizes the human VAPB-HCV NS5B interaction and reveals that NS5B C-linker is intrinsically disordered in solution but capable of binding the human VAPB-MSP domain which overlaps with those for binding HCV NS5A and human Eph receptors. PMID: 26784321 The VAPB and its interacting partners cooperatively regulate protein trafficking through the ERGIC by modulating PtdIns4P levels. PMID: 26812496 Collectively, these results not only lead to a better understanding of hVAPB function but also point to potentially relevant targets for therapeutic intervention. PMID: 25826266 results suggest that the binding of vesicle-associated membrane protein-associated protein B(VAP-B) to Rab3 GTPase activating protein 1(RAB3GAP1) is implicated in the regulation of nuclear envelope formation through ER-Golgi intermediate compartment PMID: 25612670 P56S-VAPB was found to suppress adipocyte differentiation by promoting the activation of the ATF4-CHOP pathway PMID: 25824044 In patients with familial or sporadic amyotrophic lateral sclerosis (ALS) from Portugal, Iceland and Sweden no association is found with disease and VAMP-associated protein type B (VAPB) mutations. PMID: 23971766 Findings provide new pathophysiological mechanisms of P56S VAPB that differentially affect the function and survival of corticospinal and spinal motor neurons in familial amyotrophic lateral sclerosis 8. PMID: 23771029 genetic screening for this mutation should be performed in all adult patients with lower motor neuron disease, regardless of family history because of the rarity of this disease, physicians often do not suspect it, and many cases may be missed in Brazil. PMID: 24212516 Partial or complete loss of VAPB function leads to motor deficit but is unable to trigger a full-blown amyotrophic lateral sclerosis phenotype. PMID: 23446633 this discovery provides a mechanism for ALS-causing VAPB mutants/variants to gain novel functions such as to mediate ER structure before significant accumulation of aggregates occurs. PMID: 23333387 These results suggest that changes in wild type VAPB do not play a significant role in amyotrophic lateral sclerosis cases that are not caused by VAPB mutations PMID: 23281774 Transfection of a dominant-negative form of the AAA ATPase p97/VCP stabilizes mutant VAPB, suggesting a role for this ATPase in extracting the aggregated protein from the inclusions. PMID: 22611258 structual basis of VAPC binding to HCV NS5B PMID: 22815741 This study screened a cohort of 755 sporadic ALS patients, 111 familial ALS patients (97 families), and 765 control subjects of Dutch descent for mutations in vesicle-associated membrane protein B (VAPB). PMID: 22878164 VAPB promotes breast tumor growth by modulation of Akt activity. PMID: 23049696 The binding residues have been successfully mapped out on both NS5A and VAPB, thus allowing the construct of the complex structure. PMID: 22720086 The mutation in VAPB that causes amyotrophic lateral sclerosis also causes the block of transport of nucleoporins and emerin to the nuclear envelope. PMID: 22454507 ALS mutant VAPBP56S perturbs anterograde mitochondrial axonal transport by disrupting Ca(2+) homeostasis and effecting the Miro1/kinesin-1 interaction with tubulin. PMID: 22258555 Loss of either VAPB or PTPIP51 perturbs uptake of Calcium by mitochondria and results in amyotrophic lateral sclerosis. PMID: 22131369 T46I mutant of the hVAPB MSP domain is associated with amyotrophic lateral sclerosis. PMID: 22069488 endoplasmic reticulum stress and corruption of the proteasome function might contribute to the aberrant protein homeostasis associated with hVAPB PMID: 21998752 VAPB protein levels are reduced in motor neurons derived form induced pluripotent stem cells of amyotrophic lateral sclerosis patients. PMID: 21685205 three conserved prolines in VAPA and Scs2p confers less vulnerability to mutations equivalent to the amyotrophic lateral sclerosis causing mutation as compared with VAPB, which has only two conserved prolines. PMID: 21144830 newly identified mutation in human FALS has a pathogenic effect, supporting and reinforcing the role of VAPB as a causative gene of ALS. PMID: 20940299 Mutations in SOD1, ANG, VAPB, TARDBP and FUS genes have been identified in amyotrophic lateral sclerosis. PMID: 20577002 Adeno-associated viral-mediated over-expression of both wild-type and mutated form of human VAPB selectively induces death of primary mouse motor neurons, albeit with different kinetics. PMID: 20477942 study reports the first identification of the p.P56S mutation in the VAPB gene in a non-Brazilian patient PMID: 20447143 VAPB mRNA levels were decreased in the spinal cord of ALS patients compared to controls and Expression of VAPB mRNA and protein was predominantly localised to large motor neurones. PMID: 18701194 Pro56Ser mutation of VAPB lead to amyotrophic lateral sclerosis by eliminating the native protein structure. PMID: 20377183 these results demonstrate that the amyotrophic lateral sclerosis -linked VAPB mutant causes dramatic ER restructuring that may underlie its pathogenicity in motoneurons. PMID: 20008544 the mechanism by which VAP-B(P56S) aggregates are formed and induce familial motor neuron diseases PMID: 20207736 under conditions of proteasomal inhibition, as encountered in many neurodegenerative diseases including ALS, variant VAPB proteins might accumulate in affected cells and contribute to ALS pathogenesis. PMID: 20227395 evidence that Nir (Nir1, Nir2, and Nir3)-VAP-B interactions are mediated through the conserved FFAT (two phenylalanines (FF) in acidic tract) motif present in Nir proteins PMID: 15545272 Regulation of ceramide transport protein by oxyste rbinding proteins, sterols, and VAMP reveals a novel mechanism for integrating sterol regulatory signals with ceramide transport and sphingomyelin synthesis in the Golgi apparatus. PMID: 16571669 Frequency of the detected exon variation in the VAPB gene was not significantly different between patients and controls. VAPB mutations are not a common cause of adult-onset sporadic amyotrophic lateral sclerosis. PMID: 16729899 Overexpression of wild type VAPB promotes unfolded protein response, which is a reaction of the endoplasmic reticulum to suppress accumulation of misfolded proteins. PMID: 16891305 it is suggested that VAPB mutations do not significantly contribute to the genetic causes of sporadic amyotrophic lateral sclerosis in the UK and Northern Europe PMID: 17536055 P56S mutation in VAP-B may lead to a less stable interaction of this endoplasmic reticulum protein with at least two other proteins: tubulin and GAPDH. PMID: 17540579 VAPB is abundant in motor neurons and the P56S substitution causes aggregation of mutant VAPB in immobile tubular ER clusters, perturbs FFAT-motif binding, and traps endogenous VAP in mutant aggregates, which may cause motor neuron degeneration. PMID: 17804640

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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.

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