Recombinant Human Quiescin Q6 Protein

Beta LifeScience SKU/CAT #: BLA-7519P

Recombinant Human Quiescin Q6 Protein

Beta LifeScience SKU/CAT #: BLA-7519P
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Product Overview

Host Species Human
Accession O00391
Synonym FLJ34858 hQSOX Human quiescin (Q6) mRNA, partial cds Q6 QSCN6 QSOX1 QSOX1_HUMAN Quiescin Q6 Quiescin Q6 sulfhydryl oxidase 1 Skin sulfhydryl oxidase Sox Sulfhydryl oxidase 1 Sulfhydryl oxidase 1 precursor
Description Recombinant Human Quiescin Q6 Protein was expressed in Wheat germ. It is a Protein fragment
Source Wheat germ
AA Sequence KALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKN GSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFF
Molecular Weight 37 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 Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.
Subcellular Location [Isoform 1]: Golgi apparatus membrane; Single-pass membrane protein. Secreted.; [Isoform 2]: Secreted.
Protein Families Quiescin-sulfhydryl oxidase (QSOX) family
Database References
Tissue Specificity Expressed in heart, placenta, lung, liver, skeletal muscle, pancreas and very weakly in brain and kidney.

Gene Functions References

  1. This study provides a key example of the effect of glycosylation on Golgi exit and contributes to an understanding of late secretory sorting and quality control. PMID: 29757379
  2. High QSOX1 expression correlates with tumor invasiveness PMID: 29804717
  3. High QSOX1 expression is a strong and independent factor of reduced survival in breast cancer and may represent a biomarker for aggressive disease and a potential treatment target PMID: 27562495
  4. Data indicate ebselen as an in vitro inhibitor of quiescin sulfhydryl oxidase 1 (QSOX1) enzymatic activity. PMID: 26158899
  5. QSOX1 immunoexpression was observed in the non-neoplastic cerebellum samples and the medulloblastoma samples PMID: 25908093
  6. High levels of QSOX1 RNA expression is associated with breast cancer. PMID: 23536962
  7. these studies suggest that QSOX1 is a predictive biomarker for luminal cancers and that it may be a useful target for elusive luminal B disease PMID: 23680167
  8. QSOX1 may be revealed as an important player in cancer detection and prognosis. Defining the mechanism(s) of QSOX1 activity in tumors and in in vivo models will provide important insights into how to target QSOX1 with anti-neoplastic agents. PMID: 24359107
  9. Examination of the unusual kinetics of QSOX1 toward cysteine and glutathione at low micromolar concentrations suggests that circulating QSOX1 is unlikely to significantly contribute to the oxidation of these monothiols in plasma PMID: 24468475
  10. QSOX1 may be involved in neuroblastoma differentiation and regression and may thus function as a biomarker for identifying risk groups for this neoplasm. PMID: 24704990
  11. QSOX1 is induced by hypoxic stimuli and identified that QSOX1 is a direct target of HIF-1. PMID: 24008827
  12. Data suggest that isoenzyme QSOX1A is secreted from mammalian cells despite transmembrane domain; QSOX1A is cleaved at internal sites and processed within Golgi apparatus to yield soluble enzyme that forms dimer upon cleavage of C-terminal domain. PMID: 23713614
  13. QSOX1 is a potential new prognostic marker which may prove of use in the staging of breast tumours and the stratification of breast cancer patients. PMID: 23460839
  14. QSOX1 activity was required for incorporation of laminin into the extracellular matrix (ECM) synthesized by fibroblasts, and ECM produced without QSOX1 was defective in supporting cell-matrix adhesion. PMID: 23704371
  15. crystal structure PMID: 22801504
  16. These results propose for the first time possible roles for QSOX1 in atherosclerosis. PMID: 22069028
  17. Taken together, our results suggest that the mechanism of QSOX1-mediated tumor cell invasion is by activation of MMP-2 and MMP-9. PMID: 21989104
  18. Data suggested that the C449-C452 motif was essential for the activity of human QSOX 1b; the C70-C73 motif was fundamental in electron transfer from thiol-containing substrate including reduced proteins, DTT, GSH. PMID: 21148546
  19. A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes. PMID: 20211621
  20. In the plasma peptidome of patients with ductal adenocarcinoma of the pancreas (DAP), a prominent peptide was identified from the QSOX1 parent protein. This peptide was present in 16 of 23 DAP patients and 4 of 5 patients with IPMN. PMID: 19795908
  21. Data show that the longer version of human QSOX1 protein (hQSOX1a) is a transmembrane protein localized primarily to the Golgi apparatus, and that hQSOX1a can act in vivo as an oxidase. PMID: 17331072
  22. internal redox steps studied by mutagenesis PMID: 18393449

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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