Recombinant Human Probable Threonine Protease Prss50 (PRSS50) Protein (His)

Beta LifeScience SKU/CAT #: BLC-06358P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Probable Threonine Protease Prss50 (PRSS50) Protein (His)

Beta LifeScience SKU/CAT #: BLC-06358P
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 Probable Threonine Protease Prss50 (PRSS50) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q9UI38
Target Symbol PRSS50
Species Homo sapiens (Human)
Expression System E.coli
Tag C-6His
Target Protein Sequence AGEAPGALSTADPADQSVQCVPKATCPSSRPRLLWQTPTTQTLPSTTMETQFPVSEGKVDPYRSCGFSYEQDPTLRDPEAVARRWPWMVSVRANGTHICAGTIIASQWVLTVAHCLIWRDVIYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAQRFWSWVGQANDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMWPQFRTIQEKEVIILNNKECDNFYHNFTKIPTLVQIIKSQMMCAEDTHREKFCYELTGEPLVCSMEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWIWDCLNGQALALPAPSRTLLLALPLPLSLLAAL
Expression Range 40-385aa
Protein Length Full Length of Mature Protein
Mol. Weight 45.8 kDa
Research Area Cancer
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 May be involved in proteolysis through its threonine endopeptidase activity.
Subcellular Location Endoplasmic reticulum. Note=May also localize to cytoplasmic membranes.
Protein Families Peptidase S1 family
Database References
Tissue Specificity Testis specific. Differentially expressed in some breast cancer tissues.

Gene Functions References

  1. TSP50 promotes the proliferation, migration and invasion of gastric cancer cells involving NF-kappaB dependent EMT activation. Targeting TSP50 may provide a novel therapeutic strategy for the management of gastric cancer PMID: 29361914
  2. human epidermal growth factor receptor 2 (HER-2) levels, were correlated well with TSP50/p-Samd2/3 and TSP50/p27 expression status. Thus, our studies revealed a novel regulatory mechanism underlying TSP50-induced cell proliferation and provided a new favorable intervention target for the treatment of breast cancer PMID: 28650473
  3. In patients with Colon cancer, the expression of TSP50 gene was associated with a poor prognosis. PMID: 28631709
  4. TSP50 plays a significant role in NSCLC cell proliferation and may act as a novel oncogene in the development and progression of NSCLC. PMID: 27109614
  5. Results suggest that 7P3A, which consists of 70 % 25-methoxyl-dammarane-3beta, 12beta, 20-triol and 30 % artemisinin, exhibits anti-cancer effects, in part, through downregulation of testes-specific protease 50 (TSP50) expression. PMID: 27039397
  6. Results show that TSP50 is up-regulated in laryngocarcinoma tumour tissues and its down-regulation inhibits cell proliferation, reduces cell migration and induces cell apoptosis of laryngocarcinoma in NF-KB mediated pathway. PMID: 25399078
  7. we found that some breast cancer diagnosis-associated features such as tumor size, tumor grade, estrogen receptors (ER) and progesterone receptors (PR) levels, were correlated well with TSP50/p65 and TSP50/MMP9 expression status PMID: 25811800
  8. TSP50's threonine protease activity is crucial for its effects on tumor formation. PMID: 25312478
  9. The mutations in the catalytic triad of TSP50 could significantly depressed TSP50-mediated cell proliferation and tumor formation. PMID: 25049081
  10. High TSP50 expression is associated with laryngocarcinoma. PMID: 25077921
  11. the importance of threonine 310, the most critical protease catalytic site in TSP50, to TSP50-induced cell proliferation and tumor formation PMID: 22574111
  12. TSP50 is a potential effective indicator of poor survival for colorectal carcinoma patients, especially for those with early-stage tumors. PMID: 21765952
  13. Results strongly suggest that bFGF mediates TSP50 downregulation by ERK1/2 activation, leading to the phosphorylation of Sp1 in this process. PMID: 20506264
  14. TSP50, a possible protease in human testes, is activated in breast cancer epithelial cells. PMID: 11782390
  15. TSP50 was largely downregulated in all testicular germ cell tumors. It may function in mammalian spermatogenesis. Its linear catalytic structure is similar to many serine proteases, except for a Thr-for-Ser residual catalytic site substitution. PMID: 15491742
  16. Overexpression of Sp1 and C/EBPbeta transcriptional factors upregulated the activities of the TSP50 promoter. PMID: 18462069
  17. These findings suggested that DNA methylation might regulate the TSP50 and mTSP50 gene expressions in different types of tissues and spermatic cells. PMID: 18662669

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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