Recombinant Human PIN1, His tagged
Cat.No. : | PIN1-3825H |
Product Overview : | Recombinant Human PIN1 (Q13526-1) mature form (Met 1-Glu 163), fused with a polyhistide tag at the N-terminus, was produced in E. coli. |
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Source : | E. coli |
Species : | Human |
Tag : | His |
Form : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. |
Molecular Mass : | The recombinant human PIN1 consisting of 179 amino acids and has a calculated molecular mass of 20.3 kDa. It migrates as an 21 kDa band in SDS-PAGE under reducing conditions as predicted. |
Protein Length : | Met 1-Glu 163 |
Purity : | > 90 % as determined by SDS-PAGE |
Storage : | Samples are stable for up to twelve months from date of receipt at -20°C to -80°C Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Reconstitution : | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4℃ before opening to recover the entire contents. |
Gene Name : | PIN1 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [ Homo sapiens ] |
Official Symbol : | PIN1 |
Synonyms : | PIN1; peptidylprolyl cis/trans isomerase, NIMA-interacting 1; protein (peptidyl prolyl cis/trans isomerase) NIMA interacting 1; peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; dod; PPIase Pin1; rotamase Pin1; protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1; DOD; UBL5; FLJ40239; FLJ77628; MGC10717; |
Gene ID : | 5300 |
mRNA Refseq : | NM_006221 |
Protein Refseq : | NP_006212 |
MIM : | 601052 |
UniProt ID : | Q13526 |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (7)
Ask a questionYes, studies have explored the therapeutic potential of targeting PIN1 activity. Compounds inhibiting PIN1-mediated protein isomerization have shown promise as anticancer agents in preclinical studies. However, further research is needed to develop safe and effective therapeutic interventions.
An aberrant expression of PIN1 has been observed in various types of cancer. It has been found to contribute to cancer development by promoting cell proliferation, inhibiting apoptosis, and facilitating tumor angiogenesis. Additionally, PIN1 has been implicated in regulating the activity of oncogenes and tumor suppressor genes, further highlighting its involvement in cancer progression.
The protein PIN1 is a peptidyl-prolyl cis/trans isomerase that plays a critical role in regulating the conformational changes of phosphorylated proteins, particularly those involved in cell cycle progression, DNA damage response, and gene transcription. It mediates the isomerization of proline residues, thereby impacting protein stability, protein-protein interactions, and subcellular localization, influencing various cellular processes.
The abnormal expression of PIN1 in cancer can be attributed to several molecular mechanisms. One mechanism is the dysregulation of PIN1 transcription, often caused by genetic alterations or epigenetic modifications. Another mechanism involves the dysregulation of post-translational modifications that affect PIN1 protein stability and activity. Furthermore, upstream signaling pathways, such as growth factor signaling, can activate PIN1 expression. Additionally, oncogenic transcription factors and signaling cascades can directly or indirectly enhance PIN1 expression in cancer cells.
PIN1 exerts its regulatory function through the isomerization of proline residues that precede phosphorylated serine or threonine residues. This conformational change alters the stability, interactions, and localization of proteins, consequently influencing crucial cellular processes.
PIN1 interacts with oncogenes and tumor suppressor genes at various levels to modulate their activity. PIN1 mainly exerts its effect through protein isomerization, which can induce conformational changes in target proteins. PIN1 can stabilize oncogenic proteins or promote their degradation, thus affecting their activity. Similarly, PIN1 can modify the conformation of tumor suppressor proteins, leading to altered protein interactions and functional outcomes. By regulating the activity of these key players, PIN1 can influence the overall balance between oncogenic and tumor-suppressive signaling pathways in cancer cells.
Dysregulation of PIN1 has been associated with various diseases, including cancer, neurodegenerative disorders, and aging-related pathologies. Aberrant PIN1 activity can disrupt cellular signaling pathways, contribute to uncontrolled cell growth, and impair protein quality control mechanisms, leading to pathological conditions.
Customer Reviews (3)
Write a reviewFollowing the implementation of this protein reagent, the reproducibility of my experiments has significantly improved, leaving me highly satisfied.
Approaching my research results with absolute confidence, this experimental reagent's high quality elevates my research expertise.
The dilution effect of the reagent is excellent, providing a wide measurement range.
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