Recombinant Human P53-Regulated Apoptosis-Inducing Protein 1 (TP53AIP1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08675P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human P53-Regulated Apoptosis-Inducing Protein 1 (TP53AIP1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08675P
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Product Overview

Description Recombinant Human P53-Regulated Apoptosis-Inducing Protein 1 (TP53AIP1) 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 Q9HCN2
Target Symbol TP53AIP1
Synonyms p53 regulated apoptosis inducing protein 1; p53-regulated apoptosis-inducing protein 1; P53AIP 1; p53AIP1; TP53AIP 1; TP53AIP1; TPIP1_HUMAN
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MGSSSEVSFRSAQASCSGARRQGLGRGDQNLSVMPPNGRAQTHTPGWVSPCSENRDGLLPATAPGRLCSHRGADIPSFQTHQDPVTASGSSELHADCPQFRALDRAGN
Expression Range 1-108aa
Protein Length Full Length of BC069399
Mol. Weight 38.3kDa
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 play an important role in mediating p53/TP53-dependent apoptosis.
Subcellular Location Mitochondrion.
Database References

HGNC: 29984

OMIM: 605426

KEGG: hsa:63970

STRING: 9606.ENSP00000432743

UniGene: PMID: 29359367

  • Data indicate that p53-regulated apoptosis-inducing protein 1 (p53AIP1) inhibits the proliferation of PC-3M cells, arrests cell cycle at S/G2-M phase, decreases the abilities of invasion and migration and promotes cell apoptosis. PMID: 25108434
  • These studies indicate the critical role of p53AIP1 under DNA damaging stresses for cell fate determination in rheumatoid arthritis-fibroblast-like synovioctes containing the p53R248Q mutation. PMID: 24316591
  • Apak competes with p53 for binding to inhibit p53AIP1 expression. PMID: 22334068
  • large sample size of the combined cohort rejects a high-risk effect greater than 2.2 and indicates a limited role of TP53AIP1 in prostate cancer predisposition PMID: 22457820
  • p53AIP1 regulates the mitochondrial apoptotic pathway. PMID: 12019168
  • The expression of Ki67 and p53 in various forms of leukoplakia point to the increasing instability of the genome in parallel with the severity of leukoplakia. PMID: 14707453
  • expression of the p53 mutant, R248Q, in liver cancer cells may enhance their drug resistance and upregulation of P-glycoprotein activity may contribute to this protective effect. PMID: 15004724
  • Roscovitine induced up-regulation of p53AIP1 protein and the depolarization of mitochondrial potential. PMID: 15657359
  • p53AIP1 gene is important for non-small cell lung cancer progression and may be a possible prognostic marker PMID: 17851056
  • Insufficient expression of p53AIP1 may play a role in gastric carcinogenesis in patients infected with H. pylori infection. PMID: 18277906
  • Data suggest that the combination of p53AIP1 and survivin gene expression may be a powerful tool to stratify subgroups with better or worse prognosis from the variable non-small cell lung cancer population. PMID: 19228369
  • 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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