Recombinant Human Vacuolar Protein Sorting-Associated Protein 13A (VPS13A) Protein (His-SUMO)

Name: Recombinant Human Vacuolar Protein Sorting-Associated Protein 13A (VPS13A) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09464P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Vacuolar Protein Sorting-Associated Protein 13A (VPS13A) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q96RL7
Target Symbol	VPS13A
Synonyms	VPS13A; CHAC; KIAA0986; Vacuolar protein sorting-associated protein 13A; Chorea-acanthocytosis protein; Chorein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	RPPRFFNEDGVIRPYRLRDGTGNQMLQVMENGRFAKYKYFTHVMINKTDMLMITRRGVLFVTKGTFGQLTCEWQYSFDEFTKEPFIVHGRRLRIEAKERVKSVF
Expression Range	3037-3140aa
Protein Length	Partial
Mol. Weight	28.5kDa
Research Area	Neuroscience
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 the formation or stabilization of ER-mitochondria contact sites which enable transfer of lipids between the ER and mitochondria. Negatively regulates lipid droplet size and motility. Required for efficient lysosomal protein degradation.
Subcellular Location	Mitochondrion outer membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Lysosome membrane; Peripheral membrane protein. Lipid droplet. Golgi apparatus. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle.
Protein Families	VPS13 family
Database References	HGNC: 1908 OMIM: 200150 KEGG: hsa:23230 STRING: 9606.ENSP00000353422 UniGene: Hs.459790
Associated Diseases	Choreoacanthocytosis (CHAC)
Tissue Specificity	Widely expressed. Higher expression is found in brain, heart, skeletal muscle and kidney.

Gene Functions References

Expression of cancer-specific glycan epitopes represents an excellent opportunity for diagnostics and potentially specific detection of tumors. Here, we report four proteins (LIFR, CE350, VP13A, HPT) found in sera from pancreatic cancer patients carrying aberrant glycan structures as compared to those of controls. PMID: 28244758
These results suggest that PI3P regulates the functioning of Vps13, both in protein trafficking and actin cytoskeleton organization. Attenuation of PI3P-binding ability in the mutant hVps13A protein may be one of the reasons for its mislocalization and disrupted function in cells of patients suffering from chorea-acanthocytosis . PMID: 28334785
Chorein is a stimulator of Orai1 expression and thus of store operated Ca2+ entry. PMID: 27960157
Patients with chorea-acanthocytosis carrying a VPS13A mutation present with focal, treatment-resistant seizures. PMID: 26813249
Defective chorein is accompanied by significant structural disorganization of all cytoskeletal structures. PMID: 26316086
VPS13A-depleted cells showed accumulation of autophagic markers and impaired autophagic flux PMID: 25996471
Chorein is expressed in various cancer cells. In cells with high chorein expression levels chorein silencing promotes apoptotic cell death, an effect paralleled by down-regulation of PI-3K activity and BCL-2/Bax expression ratio. PMID: 25871399
Discovery of new mutations may clarify the pathogenic roles of chorein in chorea-acanthocytosis as well as in the retina PMID: 23746940
chorein interacts with beta-adducin and beta-actin. PMID: 24129186
Data indicate functions of chorein, i.e., regulation of secretion and aggregation of blood platelets. PMID: 23568775
This study demonistrated that neuroacanthocytosis disorders has heterozygotes for mutations in the VPS13A gene. PMID: 22038564
Results reveal chorein as a novel powerful regulator of cytoskeletal architecture and cell survival, thus explaining erythrocyte misshape and possibly neurodegeneration in chorea-acanthocytosis. PMID: 22227296
these results suggest that chorein is involved in exocytosis of dense-core vesicles. PMID: 22366033
Frameshift mutations of VPS genes and losses of expression of Vps13A and Vps35 proteins are common in gastric cancers and colorectal cancers with high microsatellite instability. PMID: 21733561
identified 36 pathogenic mutations of VPS13A, 20 of which were previously unreported, including two novel copy number variations PMID: 21598378
A mutation was identified in the VPS13A gene, responsible for autosomal recessive chorea-acanthocytosis. PMID: 21987550
Founder mutation and single-nucleotid epolymorphisms in chorea-acanthocytosis in French-Canadians. PMID: 15918062
The index patient was homozygous for a 3889C>T nonsense mutation in the VPS13A gene and presented with a typical ChAc phenotype. PMID: 17673232
A Mexican family, two sister, after mutation screening of the VPS13A gene revealed homozygosity for the frameshift mutation c.3556_3557dupAC in exon 33. PMID: 17998451

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.