Recombinant Human Charged Multivesicular Body Protein 2B (CHMP2B) Protein (GST)

Name: Recombinant Human Charged Multivesicular Body Protein 2B (CHMP2B) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08653P
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 Charged Multivesicular Body Protein 2B (CHMP2B) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9UQN3
Target Symbol	CHMP2B
Synonyms	ALS17; Charged multivesicular body protein 2b; CHM2B_HUMAN; CHMP family; member 2B; CHMP2.5; CHMP2b; Chromatin modifying protein 2b; Chromatin-modifying protein 2b; DMT1; hVps2-2; Vacuolar protein sorting 2; yeast; homolog of; B; Vacuolar protein sorting 2-2; Vacuolar protein sorting-associated protein 2-2; VPS2 homolog B; Vps2-2; VPS2B
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	ASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
Expression Range	1-213aa
Protein Length	Full Length
Mol. Weight	50.8kDa
Research Area	Signal Transduction
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	Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4.
Subcellular Location	Cytoplasm, cytosol. Late endosome membrane; Peripheral membrane protein.
Protein Families	SNF7 family
Database References	HGNC: 24537 OMIM: 600795 KEGG: hsa:25978 STRING: 9606.ENSP00000263780 UniGene: PMID: 27621269 these data indicate that the neuronal expression of human CHMP2B(intron5) in areas involved in motor and cognitive functions induces progressive motor alterations associated with dementia symptoms and with histopathological hallmarks reminiscent of both amyotrophic lateral sclerosis and frontotemporal dementia. PMID: 27329763 Endogenous TMEM106B was partly sequestered in CHMP2B-positive structures. SNP T185 was more associated with CHMP2B than SNP S185, and it enhanced neurotoxicity caused by CHMP2B(Intron5) compared to S185-expressing cells. PMID: 26651479 Study showed that mutant CHMP2B causes the pathological accumulation of endolysosomal components early in the frontotemporal dementia disease course PMID: 26358247 Protein kinase CK2 alpha is involved in the phosphorylation of the ESCRT-III subunits CHMP3 and CHMP2B, as well as of VPS4B/SKD1, an ATPase that mediates ESCRT-III disassembly. PMID: 24440309 Data indicate that knockdown of syntaxin 13 (syx13) further increased the cellular toxicity caused by muaant CHMP2B (CHMP2BIntron5) expression. PMID: 24095276 CHMP2B immunoreactivity was increased in the dorsal motor nucleus of the vagus nerve in Parkinson's disease and incidental Lewy body disease brains PMID: 22989140 These findings suggest that endosomal and autophagic pathway is associated with degradation or formation of alpha-synuclein aggregates in alpha-synucleinopathy. PMID: 22947304 Subjects with CHMP2B mutation show cognitive changes dominated by executive dysfunctions, years before they fulfil diagnostic criteria of FTD. PMID: 23142962 Direct link between disease-causing mutations and the cellular phenotype in cells originating from CHMP2B mutation patients with frontotemporal dementia. PMID: 22786763 This study provided a better understanding of the cellular pathogenesis of neurodegenerative diseases associated with various missense mutations of CHMP2B as well as endocytic defects. PMID: 22521643 CHMP2B polymerization scaffolds membranes in vivo represents a first step toward demonstrating its structural role during outward membrane deformation PMID: 21926173 recent advances in our understanding of the molecular basis of CHMP2B mutations indicate that the mechanisms involved may be broadly relevant to neurodegenerative processes.[review] PMID: 21222599 A novel heterozygous variant p.Ser194Leu (c.581C>T) is found in exon 6 of the CHMP2B gene in one male patient with pure frontotemporal lobar degeneration. PMID: 20625756 The results of this study confirmed that mutations in CHMP2B are not a common cause of frontotemporal lobar degeneration. PMID: 20412296 CHMP2B is required for spine growth. Taken together, these results demonstrate that a mutant ESCRT-III subunit linked to a human neurodegenerative disease can disrupt the normal pattern of spine development. PMID: 20699355 analysis of CHMP2B mutations in lower motor neuron predominant amyotrophic lateral sclerosis PMID: 20352044 The fusion of endosomes with lysosomes is required for neuronal function suggesting a pathogenic mechanism for frontotemporal dementia caused by CHMP2B mutations. PMID: 20223751 CHMP2B can be used as a reliable marker for GVD in neurons of the AD hippocampus. PMID: 20420883 there were no significant differences in the frequencies of the IVS4 + 44C/A, 1303C/A, 1254T/C and IVS15Ex16-16C/G polymorphism haplotypes in the patient cohorts (regardless of the degree of hepatic iron deposition) compared to the control cohort PMID: 15223008 identify a mutation in CHMP2B, encoding a component of the endosomal ESCRTIII complex, and show that it results in aberrant mRNA splicing in tissue samples from affected members of family with autosomal dominant frontotermporal dementia PMID: 16041373 Mutations in CHMP2B are a rare cause of familial FTLD and may be specific to the Danish pedigree. PMID: 16431024 This studyidentified mutations (Q206H; I29V) in two patients with non-SOD1 ALS. PMID: 16807408 CHMP2B mutations are not a cause of dementia in Dutch patients with familial and sporadic frontotemporal dementia. PMID: 16941655 CHMP2B can be excluded as a susceptibility gene conferring risk to sporadic forms of frontotemporal dementia. PMID: 16979267 These data suggest that C-truncating mutations in CHMP2B might underlie the pathogenic mechanism in frontotemporal lobar degeneration. PMID: 17956895 data indicates that CHMP2B mutations are a rare cause of ALS, and no mutations were found in classic ALS phenotypes. PMID: 18270236 These data suggest that SgIII, DMT-1 and HNP-1 are implicated in cell-mediated LDL oxidation. PMID: 19150442 The specificity of DMT1 inhibition by 4 molecules in a cell line is reported. PMID: 19179627 finding suggests that mutations in CHMP2B have widespread effects throughout the brain, leading to a neuro-anatomical signature distinct from other diseases in the frontotemporal lobar degeneration spectrum PMID: 19202337 Divalent metal transporter 1 (DMT1) regulation by Ndfip1 prevents metal toxicity in human neurons. PMID: 19706893

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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.