Recombinant Human Vesicle-Associated Membrane Protein 7 (VAMP7) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10090P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Vesicle-Associated Membrane Protein 7 (VAMP7) Protein (His)

Beta LifeScience SKU/CAT #: BLC-10090P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Vesicle-Associated Membrane Protein 7 (VAMP7) Protein (His) is produced by our E.coli expression system. This is a cytoplasmic protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P51809
Target Symbol VAMP7
Synonyms FLJ53045; FLJ53762; FLJ54296; HGNC:11486; OTTHUMP00000024258; OTTHUMP00000024259; OTTHUMP00000225953; SYBL 1; SYBL1; Synaptobrevin like 1; Synaptobrevin-like protein 1; Tetanus insensitive VAMP; Tetanus neurotoxin insensitive VAMP; Tetanus-insensitive VAMP; TI VAMP; Ti-VAMP; TIVAMP; VAMP-7; VAMP7; VAMP7_HUMAN; Vesicle-associated membrane protein 7
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence AILFAVVARGTTILAKHAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKHHSENKGLDKVMETQAQVDELKGIMVRNIDLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCMKN
Expression Range 2-186aa
Protein Length Cytoplasmic Domain
Mol. Weight 25.0kDa
Research Area Cell Cycle
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 Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation.
Subcellular Location Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein. Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Cytoplasmic vesicle, phagosome membrane; Single-pass type IV membrane protein. Cell junction, synapse, synaptosome.
Protein Families Synaptobrevin family
Database References
Tissue Specificity Detected in all tissues tested.

Gene Functions References

  1. VAMP-7 participates in both platelet granule secretion and spreading and suggest a mechanism whereby VAMP-7 links granule exocytosis with actin reorganization. PMID: 25999457
  2. highlight the role that VAMP3 and VAMP7 play in selection of the pathways leading to generation of ultrastructurally different LC3 compartments PMID: 25046114
  3. increased gene dosage of VAMP7, and thus higher expression levels of its protein product, enhances estrogen receptor action in male genitourinary tissues PMID: 24880616
  4. CALM is able to sort VAMP4 and VAMP7, even though they have sorting signals for other clathrin adaptors. PMID: 23741335
  5. Overexpression of Vamp7 inhibited the heterotypic fusion with lysosomes and the homotypic fusion between individual Coxiella phagosomes and replicative vacuoles. PMID: 23217169
  6. Activation of TI-VAMP-mediated exocytosis thus relies on tyrosine phosphorylation. PMID: 23471971
  7. hVps41 and VAMP7 are specifically involved in the fusion of trans-Golgi network-derived lysosome-associated membrane protein carriers with late endosomes. PMID: 23322049
  8. In a mammalian tumor cell line a subset of VAMP7 (V-SNARE)-positive vacuoles colocalize with LC3 at the cell periphery (focal adhesions) upon starvation. PMID: 22951367
  9. Downregulation of VAMP7 expression inhibited the fusion of ATP-storing vesicles and ATP-mediated calcium wave propagation. PMID: 22188132
  10. VAMP7-SNARE motif is trapped between Varp and the VAMP7 longin domain, and hence Varp kinetically inhibits the ability of VAMP7 to form SNARE complexes PMID: 23104059
  11. These studies identify a new alpha-granule subtype expressing VAMP-7 that moves to the periphery during spreading, supporting the premise that alpha-granules are heterogeneous and demonstrating that granule exocytosis is required for platelet spreading. PMID: 22589474
  12. The endosomal trafficking and recycling of MT1-MMP was found to be dependent upon Rab7 and VAMP7, and blocking the function of these proteins reduced cell migration and invasion. PMID: 22002060
  13. Behavioral characterization studies indicate that deletion of Vamp7 exon 7 is associated with a role for VAMP7 in higher brain functions. PMID: 22323709
  14. VAMP7 is involved in many fusion processes and thus plays a more general function in NK-cell activity than VAMP4. PMID: 21805468
  15. Alternative splicing of SYBL1 by exon skipping events results in the production of a number of VAMP7 isoforms. PMID: 21609427
  16. SNARE VAMP7/TI-VAMP adopts a closed conformation PMID: 20378544
  17. Results highlight the role of TI-VAMP in the secretory pathway of a tetraspanin, and support a model in which CD82 allows EGFR entry in microdomains that control its clathrin-dependent endocytosis and signaling. PMID: 20144992
  18. TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways. PMID: 19781582
  19. A G-->C transversion in a regulatory region was found to be associated with bipolar affective disorder. PMID: 11840509
  20. In ICF (immunodeficiency, centromeric instability, facial abnormalities) syndrome SYBL1 escapes from silencing and this correlates with altered patterns of histone methylation and acetylation. PMID: 12444103
  21. results reported here clarify that a Staf-zinc finger family factor is the major nuclear protein bound to the synaptobrevin-like 1 (SYBL1) promoter region and is responsible for its regulation in HeLa cells PMID: 14672948
  22. VAMP-7 is involved in the constitutive exocytosis as a slow, minor v-SNARE, but not in lysosomal transport PMID: 16195891
  23. Data show that the insensitivity of TI-VAMP to botulinum neurotoxin B relies on at least 12 amino acid changes versus VAMP-2, which are scattered along an interface of 22 amino acid residues in length. PMID: 16430921
  24. Our results show that VAMP-7 is a crucial component of granzyme B release and target cell killing in the NK cell line YT-Indy. PMID: 18042464
  25. Data show that mature human mast cells express a specific pattern of SNARE and that VAMP-7 and VAMP-8, but not VAMP-2, are required for rapid degranulation. PMID: 18253931
  26. The participation of vesicle-associated membrane protein 7 as a partner of syntaxin 7 in VacA-induced vacuole formation is reported. PMID: 18362137
  27. Collectively, these data point to a specific role of VAMP7 in delivering MT1-MMP to sites of matrix degradation, maintaining the functional machinery required for invasion. PMID: 18571410
  28. Study demonstrates that the clathrin-mediated endocytosis of the SNARE VAMP7 is directly mediated by Hrb, a clathrin adaptor and ArfGAP. PMID: 18775314
  29. HRB is involved in clathrin-dependent endocytosis and recruits TI-VAMP in this process PMID: 18819912
  30. The present results suggest that a SNARE complex containing VAMP7 and Vti1a defines a novel traffic pathway to the cell surface in both neuronal and non-neuronal cells. PMID: 19138172
  31. show that TI-VAMP interacts with the Vps9 domain and ankyrin-repeat-containing protein Varp, a guanine nucleotide exchange factor of the small GTPase Rab21, through a specific domain herein called the interacting domain. PMID: 19745841

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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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