Recombinant Human Importin Subunit Alpha-2 (KPNA2) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-06520P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Importin Subunit Alpha-2 (KPNA2) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-06520P
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Product Overview

Description Recombinant Human Importin Subunit Alpha-2 (KPNA2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P52292
Target Symbol KPNA2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence STNENANTPAARLHRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGRTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSVFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDAVEQILPTLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELPIVTPALRAIGNIVTGTDEQTQVVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVSVLSKADFKTQKEAVWAVTNYTSGGTVEQIVYLVHCGIIEPLMNLLTAKDTKIILVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQNHENESVYKASLSLIEKYFSVEEEEDQNVVPETTSEGYTFQVQDGAPGTFNF
Expression Range 2-529aa
Protein Length Full Length of Mature Protein
Mol. Weight 62.7 kDa
Research Area Immunology
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 Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular Location Cytoplasm. Nucleus.; Endoplasmic reticulum membrane. Golgi apparatus membrane.
Protein Families Importin alpha family
Database References
Tissue Specificity Expressed ubiquitously.

Gene Functions References

  1. Development of a pipeline for automated, high-throughput analysis of PSPC1 paraspeckle protein isoforms reveals specific roles for KPNA2, KPNA4 and KPNA6 proteins. PMID: 28240251
  2. the present study demonstrated that the function of KPNA2 in the process of autophagy may be p53dependent, and by regulating the translocation of p53, KPNA2 can support autophagy to promote the chemoresistance and metastasis of oral squamous cell carcinoma (OSCC) cells. PMID: 29781035
  3. KPNA2 expression may be a useful prognostic and predictive marker of gemcitabine sensitivity and survival. PMID: 28178675
  4. KPNA2 was an essential factor promoting hepatocellular carcinoma and unraveled potential molecular pathways and networks underlying KPNA2-induced hepatocellular carcinogenesis. PMID: 28422734
  5. we confirmed that up-regulated KPNA2 and OCT4 expression is a common feature of bladder cancer that is correlated with increased aggressive tumor behavior. Also, we propose that KPNA2 regulates the process of OCT4 nuclear transportation in bladder cancer. PMID: 27611951
  6. KPNA2 overexpression was associated with poor OS in East-Asian patients and European patients, as well as patients with gastric and colorectal cancer.[meta-analysis] PMID: 27974678
  7. our results show for the first time that KPNA2 is transcriptionally and post-translationally regulated by the mTOR pathway and provide new insights into targeted therapy for non-small cell lung cancer PMID: 27009856
  8. KPNA2 was associated with tumorigenesis and cancer progression in CRC cells; high KPNA2 expression was associated with increased cell proliferation, migration, invasion, and semisolid agar colony formation. PMID: 28875407
  9. that the interactions observed between TNRC6A and importin-alpha are conserved between mouse and human complexes. Our results highlight the ability of monopartite cNLS sequences to maximise contacts at the importin-alpha major binding site, as well as regions outside the main binding cavities. PMID: 28837617
  10. The authors identified Importin-alpha1 to bind to Coxiella burnetii AnkG and concluded that binding of AnkG to p32 and Importin-alpha1 is essential for its migration into the nucleus. PMID: 27328359
  11. the crystal structure of the nuclear import adaptor importin-alpha1 bound to the nuclear localization signal (NLS) of EBNA-LP that shows EBNA-LP residues 44-RRVRRR-49 binding to the major NLS-binding site at the P0-P5 positions. PMID: 28383161
  12. High serum karyopherin alpha 2 levels (>485 microg/mL) correlated with International Federation of Gynecology and Obstetrics stage ( p < 0.0001), lymphatic metastasis ( p = 0.045), overall survival ( p = 0.001), and disease-free progression ( p = 0.006). Serum karyopherin alpha 2 represents a potential diagnostic biomarker for epithelial ovarian carcinoma. PMID: 28651492
  13. p53/p21Cip1/Waf1/p16INK4a may be an important pathway involved in the function of KPNA2 in tongue squamous cell carcinoma (TSCC) CAL-27 cells. PMID: 27109484
  14. Results demonstrated that radiation-induced dying colorectal cancer cells released considerable amounts of KPNA2 that induce the maturation and activation of DCs for synergistic antitumor effect of radiation. PMID: 27107455
  15. These results suggest that the selected aptamers (76 and 72) warrant further study to explore not only their application in cancer diagnosis but also their use as a specific reagent to potentially block KPNA2-dependent nuclear transport of macromolecules across the nuclear membrane. PMID: 27154959
  16. anti-importin alpha1 antibody treatment suppressed the importin alpha1-FGF1 complex formation and ERK1/2 activation, resulting in decreased cell growth. This study provides novel evidence that functional importin alpha1 is located at the cell surface, where it accelerates the proliferation of cancer cells. PMID: 26887791
  17. The combination of low nuclear and cytoplasmic KPNA2 expression is associated with adverse outcome in head and neck squamous cell carcinoma treated with radio(chemo)therapy. PMID: 26884852
  18. provided support for a link between autophagy and epithelial-to-mesenchymal (-like) transition status in WT TP53 glioblastoma cells and provided evidence for the signaling pathway (MIR517C-KPNA2-cytoplasmic TP53) involved in attenuating autophagy PMID: 26553592
  19. Suggest that KPNA2 may play a key role in the inflammation process of rheumatoid arthritis via NF-kappaB P65 signal transduction pathway. PMID: 26135850
  20. KPNA2 might play an important role in colorectal carcinogenesis and functions as a novel prognostic indicator and a potential therapeutic target for colorectal cancer. PMID: 26626145
  21. High KPNA2 expression was found to be associated with poor prognosis and resistance to hyperthermochemoradiation therapy (HCRT). PMID: 26663089
  22. A novel role of karyopherin alpha 2 in cell migration through the regulation of vimentin-pErk protein complex levels in lung cancer. PMID: 25728791
  23. High KPNA2 immunoreactivity is a predictor of bladder recurrence and poor survival in patients with upper tract urothelial carcinoma treated with radical nephroureterectomy. PMID: 25956057
  24. High KPNA2 expression is associated with osteoarthritis. PMID: 26209501
  25. Crystal structure of human importin-alpha1 (Rch1), revealing a potential autoinhibition mode involving homodimerization. PMID: 25658636
  26. OPN, SPINK1, GPC3 and KNPA2 were significantly over-expressed in HCC tissues. These genes may be useful in developing future biomarkers and therapeutic strategies for HCC PMID: 25862856
  27. This study provides further evidence for the complexity of DDR mechanism in BC, and that KNPA2 has a role in the aberrant subcellular localisation of DDR proteins with subsequent impaired function. PMID: 25989275
  28. KPNA2 was overexpressed in esophageal squamous cell carcinoma tissue and cell lines. Serum KPNA2 was higher in ESCC patients than in controls. KPNA2 knockdown inhibited cell proliferation and colony formation ability and induced a G2/M phase arrest. PMID: 25109899
  29. Aberrant expression of nuclear KPNA2 is correlated with early recurrence and poor prognosis in patients with small hepatocellular carcinoma after hepatectomy. PMID: 25031071
  30. The nuclear import of PLAG1 by KPNA2 is essential for the role of KPNA2 in HCC cells. PMID: 25060425
  31. study analyzed nuclear expression of karyopherin a2 in meningiomas; expression correlated with histological grade and proliferative activity; recurrent tumors expressed significantly higher levels of karyopherin a2 when compared to primary growths PMID: 24664371
  32. KPNA2 and CDK1 expression levels may discriminate between estrogen receptor positive patients of high and low risk of disease recurrence. PMID: 24799281
  33. a significant correlation of KPNA2 expression and tumour aggressiveness in a large variety of other solid tumour entities PMID: 24930886
  34. The cellular apoptosis susceptibility/importin-alpha1 transport cycle is linked to X-linked inhibitor (XIAP) and is required to maintain tumor cell survival in hepatocellular carcinoma. PMID: 24799195
  35. Identified a strong link between high KPNA2 expression and early PSA recurrence in prostate cancer patients treated with radical prostatectomy. PMID: 23887301
  36. High NBS1 expression was linked to biochemical recurrence in ERG-negative and PTEN non-deleted cancers, which was largely driven by high KPNA2 karyopherin alpha 2 expression. PMID: 24510842
  37. These findings demonstrate that rotavirus probably employs a novel strategy to inhibit interferon-induced STAT signalling, which acts after STAT1/STAT2 activation and binding to importin-alpha. PMID: 24814927
  38. Karyopherin alpha2 is essential for rRNA transcription and protein synthesis in proliferative keratinocytes. PMID: 24098495
  39. Oct4 and KPNA2 play an important role in non-small-cell lung cancer progression. PMID: 24070213
  40. Importin alpha1 and alpha7 are positive regulators of human-like polymerase activity and pathogenicity beyond their role in nuclear transport. PMID: 22275867
  41. IGFBP-2 possesses a functional nuclear localization signal sequence and IGFBP-2 actively translocates into the nucleus by a classical nuclear import mechanism, involving formation of IGFBP-2 complexes with importin-alpha. PMID: 23435424
  42. SEPT9 isoform 1 is required for the association between HIF-1alpha and importin-alpha to promote efficient nuclear translocation. PMID: 24067372
  43. KPNA2 has an important role in promoting proliferation and tumorigenicity of epithelial ovarian carcinoma through upregulation of c-myc and suppression of FOXO3A. PMID: 23907459
  44. This work defines an inflammatory signature shared by seven epithelial cancer types and KPNA2 as a consistently up-regulated protein in cancer. PMID: 23536776
  45. Nuclear karyopherin-alpha2 expression in primary lesions and metastatic lymph nodes was associated with poor prognosis and progression in gastric cancer. PMID: 23749771
  46. Tpr import is mediated by the most abundant import receptor, KPNA2, which binds the bipartite NLS in Tpr with nanomolar affinity PMID: 23649804
  47. Overexpression of KPNA2 correlates with gastric adenocarcinoma. PMID: 23283818
  48. The KPNA2-regulating protein profiles in an adenocarcinoma cell line, were analyzed. PMID: 22843992
  49. KPNA2 expression may have potential as a novel diagnostic and prognostic biomarker for astrocytic gliomas. PMID: 22772608
  50. Overexpression of karyopherin 2 (KPNA2) in human ovarian malignant germ cell tumor correlates with poor prognosis. PMID: 22962582

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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.

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