Anti-KPNA4 (C-terminal) polyclonal antibody

Name: Anti-KPNA4 (C-terminal) polyclonal antibody
SKU: DPABH-16728
Rating: 5 (1 reviews)

Goat anti-Human KPNA4 (C-terminal) polyclonal antibody for IHC-P, WB

Write a review

COA

SDS

Datasheet

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Mouse; Human

Immunogen

Peptide with sequence NSSANVPTEGFQF, from C Terminus of the protein sequence according to NP_002259

Conjugate

Unconjugated

Applications

Application Notes

IHC-P: 1 - 2 μg/ml; WB: 0.2 - 1 μg/ml.

Target

Alternative Names

KPNA4; karyopherin alpha 4 (importin alpha 3); importin subunit alpha-4; IPOA3; MGC12217; MGC26703; QIP1; SRP3; importin alpha Q1; karyopherin subunit alpha-4; FLJ31113;

Entrez Gene ID

3840

UniProt ID

O00629

Product Background

Antigen Description

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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a nonclassical NLS.

Pathway

Antiviral mechanism by IFN-stimulated genes; Cytokine Signaling in Immune system; ISG15 antiviral mechanism; Immune System; Interferon Signaling;

Citations

Have you cited DPABH-16728 in a publication? Let us know and earn a reward for your research.

Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Porcine circovirus type 2 inhibits inter-beta expression by targeting Karyopherin alpha-3 in PK-15 cells

VIROLOGY

Authors: Li, Jiansheng; Lu, Mingqing; Huang, Bei; Lv, Yingjun

Abstract

Interferon (IFN)-mediated antiviral response is an important part of host defense. Previous studies reported that porcine circovirus type 2 (PCV2) inhibits interferon production, but the mechanism is still poorly understood. In this study, PCV2 suppresses IFN-beta and IRF3 promoters and mRNA level of IFN-beta induced by ISD or Poly(I:C), but has no effect on the activation of AP-1 and NF-kB. Furthermore, PCV2 decreases the mRNA level of IFN-beta and IFN-beta promoter activity driven by STING, TBK1, IRF3, and IRF3/5D, and causes a reduction in the protein level of nuclear p-IRF3. In addition, PCV2 interrupts the interaction of KPNA3, rather than KPNA4, with p-IRF3. Overexpression of KPNA3 restores IFN-beta promoter activity. These results indicate that PCV2 disrupts the interaction of KPNA3 with p-IRF3 and blocks p-IRF3 translocation to the nucleus, thereby inhibiting IFN-beta induction in PK-15 cells.

Genetic loss of importin alpha 4 causes abnormal sperm morphology and impacts on male fertility in mouse

FASEB JOURNAL

Authors: Miyamoto, Yoichi; Sasaki, Mitsuho; Miyata, Haruhiko; Monobe, Yoko; Nagai, Masahiro; Otani, Mayumi; Whiley, Penny A. F.; Morohoshi, Akane; Oki, Shinya; Matsuda, Junichiro; Akagi, Ken-ichi; Adachi, Jun; Okabe, Masaru; Ikawa, Masahito; Yoneda, Yoshihiro; Loveland, Kate L.; Oka, Masahiro

Abstract

Importin alpha proteins play a central role in the transport of cargo from the cytoplasm to the nucleus. In this study, we observed that male knock-out mice for importin alpha 4, which is encoded by theKpna4gene (Kpna4(-/-)), were subfertile and yielded smaller litter sizes than those of wild-type (WT) males. In contrast, mice lacking the closely related importin alpha 3 (Kpna3(-/-)) were fertile. In vitro fertilization and sperm motility assays demonstrated that sperm fromKpna4(-/-)mice had significantly reduced quality and motility. In addition, acrosome reaction was also impaired inKpna4(-/-)mice. Transmission electron microscopy revealed striking defects, including abnormal head morphology and multiple axoneme structures in the flagella ofKpna4(-/-)mice. A five-fold increase in the frequency of abnormalities inKpna4(-/-)mice compared toWTmice indicates the functional importance of importin alpha 4 in normal sperm development. Moreover, Nesprin-2, which is a component of the linker of nucleus and cytoskeleton complex, was expressed at lower levels in sperm fromKpna4(-/-)mice and was localized with abnormal axonemes, suggesting incorrect formation of the nuclear membrane-cytoskeleton structure during spermiogenesis. Proteomics analysis ofKpna4(-/-)testis showed significantly altered expression of proteins related to sperm formation, which provided evidence that genetic loss of importin alpha 4 perturbed chromatin status. Collectively, these findings indicate that importin alpha 4 is critical for establishing normal sperm morphology in mice, providing new insights into male germ cell development by highlighting the requirement of importin alpha 4 for normal fertility.