Recombinant Human Sulfhydryl Oxidase 1 (QSOX1) Protein (His-GST&Myc)

Name: Recombinant Human Sulfhydryl Oxidase 1 (QSOX1) Protein (His-GST&Myc)
Brand: Beta LifeScience
SKU: BLC-07470P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Sulfhydryl Oxidase 1 (QSOX1) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O00391
Target Symbol	QSOX1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-GST&C-Myc
Target Protein Sequence	CAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEE
Expression Range	101-175aa
Protein Length	Partial
Mol. Weight	43.4 kDa
Research Area	Cell Biology
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	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	HGNC: 9756 OMIM: 603120 KEGG: hsa:5768 STRING: 9606.ENSP00000356574 UniGene: Hs.744925
Tissue Specificity	Expressed in heart, placenta, lung, liver, skeletal muscle, pancreas and very weakly in brain and kidney.

Gene Functions References

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
High QSOX1 expression correlates with tumor invasiveness PMID: 29804717
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
Data indicate ebselen as an in vitro inhibitor of quiescin sulfhydryl oxidase 1 (QSOX1) enzymatic activity. PMID: 26158899
QSOX1 immunoexpression was observed in the non-neoplastic cerebellum samples and the medulloblastoma samples PMID: 25908093
High levels of QSOX1 RNA expression is associated with breast cancer. PMID: 23536962
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
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
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
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
QSOX1 is induced by hypoxic stimuli and identified that QSOX1 is a direct target of HIF-1. PMID: 24008827
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
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
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
crystal structure PMID: 22801504
These results propose for the first time possible roles for QSOX1 in atherosclerosis. PMID: 22069028
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
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
A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes. PMID: 20211621
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
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
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.