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Rat Anti-KPNA2 Recombinant Antibody (1A6) (CBMAB-K1473-LY)


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Summary

Host Animal
Rat
Specificity
Human
Clone
1A6
Antibody Isotype
IgG2a
Application
ICC, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
50% glycerol
Concentration
1 mg/ml
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Karyopherin Subunit Alpha 2
Introduction
The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein 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. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]
Entrez Gene ID
3838
UniProt ID
P52292
Alternative Names
Karyopherin Subunit Alpha 2; Karyopherin Alpha 2 (RAG Cohort 1; Importin Alpha 1); RAG Cohort Protein 1; SRP1-Alpha; RCH1; Karyopherin Subunit Alpha-2; Importin Subunit Alpha-1; Importin Subunit Alpha-2; Karyopherin Alpha 2;
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.
Biological Process
DNA metabolic processManual Assertion Based On ExperimentTAS:ProtInc
Entry of viral genome into host nucleus through nuclear pore complex via importinManual Assertion Based On ExperimentIMP:MGI
NLS-bearing protein import into nucleusManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of viral life cycleManual Assertion Based On ExperimentIMP:MGI
Postsynapse to nucleus signaling pathwayManual Assertion Based On ExperimentIDA:SynGO
Regulation of DNA recombinationManual Assertion Based On ExperimentTAS:ProtInc
Cellular Location
Cytoplasm
Nucleus
Endoplasmic reticulum membrane
Golgi apparatus membrane
(Microbial infection) Retained in ER/Golgi membranes upon interaction with SARS-COV virus ORF6 protein.
More Infomation

Jia, Y., Wang, Q., Liang, M., & Huang, K. (2022). KPNA2 promotes angiogenesis by regulating STAT3 phosphorylation. Journal of translational medicine, 20(1), 1-15.

Cui, X., Wang, H., Wu, X., Huo, K., & Jing, X. (2021). Increased expression of KPNA2 predicts unfavorable prognosis in ovarian cancer patients, possibly by targeting KIF4A signaling. Journal of Ovarian Research, 14(1), 1-11.

Sun, Y., Li, W., Li, X., Zheng, H., Qiu, Y., & Yang, H. (2021). Oncogenic role of karyopherin α2 (KPNA2) in human tumors: a pan-cancer analysis. Computers in Biology and Medicine, 139, 104955.

Zhou, K. X., Huang, S., Hu, L. P., Zhang, X. L., Qin, W. T., Zhang, Y. L., ... & Zhang, Z. G. (2021). Increased nuclear transporter KPNA2 contributes to tumor immune evasion by enhancing PD-L1 expression in PDAC. Journal of immunology research, 2021.

Han, Y., & Wang, X. (2020). The emerging roles of KPNA2 in cancer. Life sciences, 241, 117140.

Xiang, S., Wang, Z., Ye, Y., Zhang, F., Li, H., Yang, Y., ... & Liu, Y. (2019). E2F1 and E2F7 differentially regulate KPNA2 to promote the development of gallbladder cancer. Oncogene, 38(8), 1269-1281.

Ma, A., Tang, M., Zhang, L., Wang, B., Yang, Z., Liu, Y., ... & Liu, Y. (2019). USP1 inhibition destabilizes KPNA2 and suppresses breast cancer metastasis. Oncogene, 38(13), 2405-2419.

Guo, X., Wang, Z., Zhang, J., Xu, Q., Hou, G., Yang, Y., ... & Liu, H. (2019). Upregulated KPNA2 promotes hepatocellular carcinoma progression and indicates prognostic significance across human cancer types. Acta biochimica et biophysica Sinica, 51(3), 285-292.

Li, J., Liu, Q., Liu, Z., Xia, Q., Zhang, Z., Zhang, R., ... & Xin, T. (2018). KPNA2 promotes metabolic reprogramming in glioblastomas by regulation of c-myc. Journal of Experimental & Clinical Cancer Research, 37(1), 1-15.

Huang, L., Zhou, Y., Cao, X. P., Lin, J. X., Zhang, L., Huang, S. T., & Zheng, M. (2018). KPNA2 promotes migration and invasion in epithelial ovarian cancer cells by inducing epithelial-mesenchymal transition via Akt/GSK-3β/Snail activation. Journal of Cancer, 9(1), 157.

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For research use only. Not intended for any clinical use.

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