Recombinant Human Programmed Cell Death Protein 5 (PDCD5) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03939P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Programmed Cell Death Protein 5 (PDCD5) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03939P
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Product Overview

Description Recombinant Human Programmed Cell Death Protein 5 (PDCD5) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O14737
Target Symbol PDCD5
Synonyms PDCD5; PDCD5_HUMAN; Programmed cell death protein 5; Protein TFAR19; TF 1 cell apoptosis related protein 19; TF-1 cell apoptosis-related protein 19; TFAR19; TFAR19 novel apoptosis-related
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MADEELEALRRQRLAELQAKHGDPGDAAQQEAKHREAEMRNSILAQVLDQSARARLSNLALVKPEKTKAVENYLIQMARYGQLSEKVSEQGLIEILKKVSQQTEKTTTVKFNRRKVMDSDEDDDY
Expression Range 1-125aa
Protein Length Full Length
Mol. Weight 41.2kDa
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 May function in the process of apoptosis.
Protein Families PDCD5 family
Database References
Tissue Specificity Widely expressed. Highest levels in heart, testis, kidney, pituitary gland, adrenal gland and placenta.

Gene Functions References

  1. Collectively, these data demonstrate that PPEF-1 plays a pivotal role in tumorigenesis of lung cancer cells by reducing PDCD5-mediated genotoxic stress responses. PMID: 28051100
  2. In the high malignant group the PDCD4 mRNA and PDCD5 mRNA expressions were significantly decreased compared with the low malignant group and the control group. PDCD4 mRNA and PDCD5 mRNA expressions are promising targets for the diagnosis and treatment of glioma. PMID: 29921407
  3. serum PDCD5 levels reflect endothelial NO production and are correlated with diabetes mellitus, high-density lipoprotein cholesterol, and coronary calcium PMID: 29588416
  4. As a transcriptional activator, PITX1 regulates apoptosis-related genes, including PDCD5, during gastric carcinogenesis. PMID: 29734189
  5. DKK-1 and PDCD5 can be independent predictors of overall survival in patients suffering from chondrosarcoma. PMID: 27255549
  6. Endogenous PDCD5 overexpression accelerated multiple myeloma cell apoptosis under dexamethasone treatment. PMID: 26617773
  7. Studies indicate that programmed cell death 5 (PDCD5) interacts with the tumor protein p53 (p53) pathway to promote cell apoptosis. PMID: 26433055
  8. This review describes what is known about PDCD5 and its cellular functions. [review] PMID: 26775586
  9. The results suggest a role of PDCD5 in the regulation of p53 function but unrelated to cell cycle arrest or apoptosis, at least in the cell types investigated. PMID: 26062895
  10. PDCD5 selectively mediates HDAC3 dissociation from p53, which induces HDAC3 cleavage and ubiquitin-dependent proteasomal degradation. This is a a mechanism for p53 activation via PDCD5-dependent HDAC3 decay under genotoxic stress conditions. PMID: 26077467
  11. PDCD5 expression is negatively correlated with disease progression and stage in ovarian cancer. PMID: 25881604
  12. These findings uncovered an apoptotic signaling cascade linking YAF2, PDCD5, and TP53 during genotoxic stress responses. PMID: 25603536
  13. Transgenic mice with systemic overexpression of human PDCD5 were protected from cardiac remodeling. PMID: 25881505
  14. Findings have uncovered an apoptotic signaling cascade linking PDCD5, OTUD5, and p53 during genotoxic stress responses. PMID: 25499082
  15. Authors identified DNAJB1 as a negative regulator of PDCD5-mediated apoptosis and found that the apoptosis network of PDCD5 regulates cancer cell death. PMID: 25444898
  16. We confirmed that PDCD5 overexpression stimulated the promoter activities of KLF9 by luciferase reporter assays. PMID: 24173774
  17. PDCD5 is necessary and sufficient for NF-kappaB p65 mediated apoptosis PMID: 24343129
  18. The expression of PDCD5 and its protein were shown to be reduced in laryngeal squamous cell carcinoma. The functional importance of PDCD5 as a regulating agent in cell apoptosis suggests that it may play a key role in tumour pathogenesis and development. PMID: 24265335
  19. PDCD5 bound the apical domain of the CCTbeta subunit, projecting above the folding cavity without entering it. Like PDCD5, beta-tubulin also interacts with the CCTbeta apical domain, but a second site is found at the sensor loop deep within the folding cavity. PMID: 24375412
  20. PDCD5 could be considered as a reliable marker of favorable prognosis of HCC patients PMID: 23807738
  21. PDCD5 may contribute to maintain a basal pool of p53 proteins in unstressed conditions, but upon DNA damage it functions as a co-activator of p53 to regulate transcription and cell cycle arrest. PMID: 22914926
  22. Insulin-like growth factor 1 down-regulates programmed cell death 5 in osteoarthritis chondrocytes. PMID: 23322062
  23. Data indicate that the expressions of genes PDCD5 and TIMP2 were consistent with their DNA methylation profiles. PMID: 23369618
  24. a correlation between increased levels of PDCD5 in serum and liver disease progression and indicate the potential utility of serum PDCD5 as a biomarker for monitoring liver injury. PMID: 23656249
  25. Transgenic PDCD5 plays an antitumor role with increased expression, suppressing skin cancer development. PMID: 23688867
  26. Plasma and synovial fluid PDCD5 expression levels are inversely associated with TNF-alpha and disease activity in patients with rheumatoid arthritis. PMID: 23327497
  27. results suggest that PDCD5 expression plays a significant role in the malignant progression of human gastrointestinal stromal tumors and may be a key inhibitory factor PMID: 22965478
  28. PDCD5 participates in the inflammatory process of asthmatic airway. Its abnormal expression may be associated with the uncontrolled state of asthmatics. PMID: 22883196
  29. PDCD5 promotes chemosensitivity by activating the mitochondria-related apoptotic pathway. PMID: 22688731
  30. This study is the first providing evidence that PDCD5 plays an important role in cardiac remodeling. PMID: 22253891
  31. the PDCD5 binding site on p53 is localized within residues 41-56 of p53 TAD2 subdomain while p53 binds preferentially to the positively charged surface region around the C-terminals of helices alpha3 and alpha5 and the N-terminal of helix alpha4 of PDCD5 PMID: 22372375
  32. The effect of recombinant human PDCD5 was also investigated and shown to sensitize cells to DNA damage by promoting caspase-3 activity. PMID: 22261045
  33. Abnormal expression of pdcd5 may be involved in the pathogenesis of multiple myeloma. PMID: 20561417
  34. Lost or reduced PDCD5 expression may contribute to the pathogenesis of human serous cystadenocarcinomas. PMID: 21165576
  35. Downregulated expression of programmed cell death 5 is associated with chondrosarcoma. PMID: 20872801
  36. Data show that the number of apoptotic cells in renal tubuli with lupus nephritis correlated negatively with the intensity of PDCD5 expression. PMID: 16083554
  37. Overexpression of PDCD5 could enhance apoptosis of rheumatoid arthritis fibroblast-like synoviocytes induced by triptolide. PMID: 19088824
  38. protein overexpression enhance apoptosis in triptolide-induced synoviocytes of rheumatoid arthritis patients PMID: 20047520
  39. By downregulating apoptosis, low PDCD5 expression may play an important role in the occurrence and development of PAROSTATIC NEOPLASM. PMID: 20120772
  40. PDCDS was highly expressed in some ragged red fibers in patients with limb-girdle type mitochondrial myopathy and chronic progressive external ophthalmoplegia. PMID: 19957502
  41. Results imply that the PDCD5 gene may be a target gene under the control of some important apoptosis-related transcriptional factors during the cell apoptosis. PMID: 15033527
  42. The effects of the secondary structure of PDCD5 on its tertiary structure and function are reported. PMID: 16083422
  43. -27G/-11A SNP is associated with reduced PDCD5 promoter activity and increased susceptibility to chronic myelogenous leukemia. PMID: 16361542
  44. Could play an important role in regulation of apoptotic processes in gastric cancer cells and gastric tumors. PMID: 16547588
  45. PDCD5 may be involved in the pathogenesis of rheumatoid arthritis. PMID: 17468978
  46. PDCD5 expression in bone marrow nucleated cells in untreated acute myeloid leukemia patients is lower than in normal controls. PMID: 17605845
  47. exogenous PDCD5 expression enhances the chemosensitivity of K562 leukemia cells to either low or high doses of idarubicin in vitro, resulting in increased apoptosis. PMID: 18401719
  48. Reduced expression of PDCD5 is associated with high-grade astrocytic gliomas PMID: 18695908
  49. PDCD5 contributes to maintaining a basal pool of Tip60 and its HAT activity PMID: 19308289
  50. Studies of structure-function relationship of PDCD5 by multidimensional NMR methods and flow cytometer and fluorescence microscopey. PMID: 19358820

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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