Recombinant Human KPNA2 Protein (N-6His)

Name: Recombinant Human KPNA2 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-1485NP
Availability: InStock

BL-1485NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Karyopherin Subunit Alpha-2 is produced by our E.coli expression system and the target gene encoding Met1-Phe529 is expressed with a 6His tag at the N-terminus.
Accession	P52292
Synonym	Importin Subunit Alpha-2; Karyopherin Subunit Alpha-2; RAG Cohort Protein 1; SRP1-Alpha; KPNA2; RCH1; SRP1
Gene Background	Karyopherin Subunit α-2 (KPNA2) belongs to the importin alpha family. KPNA2 is widely expressed in many tissues and contains an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. KPNA2 interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination. KPNA2 functions in nuclear protein importantly as an adapter protein for nuclear receptor KPNB1.
Molecular Mass	60.04 KDa
Apmol Mass	60 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 1mM DTT, 20% Glycerol, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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	HGNC: 6395 OMIM: 600685 KEGG: hsa:3838 STRING: 9606.ENSP00000332455 UniGene: PMID: 28240251 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 KPNA2 expression may be a useful prognostic and predictive marker of gemcitabine sensitivity and survival. PMID: 28178675 KPNA2 was an essential factor promoting hepatocellular carcinoma and unraveled potential molecular pathways and networks underlying KPNA2-induced hepatocellular carcinogenesis. PMID: 28422734 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 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 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 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 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 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 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 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 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 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 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 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 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 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 Suggest that KPNA2 may play a key role in the inflammation process of rheumatoid arthritis via NF-kappaB P65 signal transduction pathway. PMID: 26135850 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 High KPNA2 expression was found to be associated with poor prognosis and resistance to hyperthermochemoradiation therapy (HCRT). PMID: 26663089 A novel role of karyopherin alpha 2 in cell migration through the regulation of vimentin-pErk protein complex levels in lung cancer. PMID: 25728791 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 High KPNA2 expression is associated with osteoarthritis. PMID: 26209501 Crystal structure of human importin-alpha1 (Rch1), revealing a potential autoinhibition mode involving homodimerization. PMID: 25658636 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 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 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 Aberrant expression of nuclear KPNA2 is correlated with early recurrence and poor prognosis in patients with small hepatocellular carcinoma after hepatectomy. PMID: 25031071 The nuclear import of PLAG1 by KPNA2 is essential for the role of KPNA2 in HCC cells. PMID: 25060425 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 KPNA2 and CDK1 expression levels may discriminate between estrogen receptor positive patients of high and low risk of disease recurrence. PMID: 24799281 a significant correlation of KPNA2 expression and tumour aggressiveness in a large variety of other solid tumour entities PMID: 24930886 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 Identified a strong link between high KPNA2 expression and early PSA recurrence in prostate cancer patients treated with radical prostatectomy. PMID: 23887301 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 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 Karyopherin alpha2 is essential for rRNA transcription and protein synthesis in proliferative keratinocytes. PMID: 24098495 Oct4 and KPNA2 play an important role in non-small-cell lung cancer progression. PMID: 24070213 Importin alpha1 and alpha7 are positive regulators of human-like polymerase activity and pathogenicity beyond their role in nuclear transport. PMID: 22275867 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 SEPT9 isoform 1 is required for the association between HIF-1alpha and importin-alpha to promote efficient nuclear translocation. PMID: 24067372 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 This work defines an inflammatory signature shared by seven epithelial cancer types and KPNA2 as a consistently up-regulated protein in cancer. PMID: 23536776 Nuclear karyopherin-alpha2 expression in primary lesions and metastatic lymph nodes was associated with poor prognosis and progression in gastric cancer. PMID: 23749771 Tpr import is mediated by the most abundant import receptor, KPNA2, which binds the bipartite NLS in Tpr with nanomolar affinity PMID: 23649804 Overexpression of KPNA2 correlates with gastric adenocarcinoma. PMID: 23283818 The KPNA2-regulating protein profiles in an adenocarcinoma cell line, were analyzed. PMID: 22843992 KPNA2 expression may have potential as a novel diagnostic and prognostic biomarker for astrocytic gliomas. PMID: 22772608 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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Recombinant Human KPNA2 Protein (N-6His)

Recombinant Human KPNA2 Protein (N-6His)

Product Overview

Target Details

FAQs