Human ABCB9 blocking peptide

Name: Human ABCB9 blocking peptide
SKU: CDBP0266
Rating: 5 (1 reviews)

Synthetic Human ABCB9 blocking peptide for Apuri, BL, ELISA

COA

SDS

Datasheet

Summary

Product Overview

Blocking/Immunizing peptide for anti-ABCB9/TAPL antibody

Target

ABCB9 / TAPL

Nature

Synthetic

Tag/Conjugate

Unconjugated

Application Notes

For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not for human or animal consumption.

Format

Lyophilized powder

Preservative

None

Storage

Shipped at ambient temperature, store at -20°C.

Entrez Gene ID

23457

Antigen Description

The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MDR/TAP subfamily. Members of the MDR/TAP subfamily are involved in multidrug resistance as well as antigen presentation. This family member functions in the translocation of peptides from the cytosol into the lysosomal lumen. Alternative splicing of this gene results in distinct isoforms which are likely to have different substrate specificities.

Function

ATP binding; ATP binding; ATPase activity; ATPase activity, coupled to transmembrane movement of substances; MHC class I protein binding; TAP1 binding; TAP2 binding; nucleotide binding; oligopeptide-transporting ATPase activity; peptide antigen binding; p

Synonyms

ABCB9; ATP-binding cassette, sub-family B (MDR/TAP), member 9; ATP-binding cassette sub-family B member 9; EST122234; TAP-like protein; ABC transporter 9 protein; TAPL; KIAA1520;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

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Customer Reviews

References

miR-196a Promotes Proliferation and Inhibits Apoptosis of Immature Porcine Sertoli Cells

DNA AND CELL BIOLOGY

Authors: Zhang, Shaoxuan; Guo, Jia; Liang, Mengdi; Qi, Jiajia; Wang, Zhenbo; Jian, Xinrui; Zhang, Zhibin; Sun, Boxing; Li, Zhaohua

Abstract

Our previous study showed that the expression of miR-196a was significantly higher in immature porcine testes than in mature porcine testes. However, the role of miR-196a in immature Sertoli cells remains unclear. In this study, miR-196a mimics, miR-196a inhibitor, and microRNA-small hairpin negative control (miRNA-ShNC) were transfected into immature Sertoli cells, respectively. Subsequently, the cell cycle and apoptosis rate of the immature Sertoli cells were measured by flow cytometry, and the viability of the Sertoli cells was measured by the MTS assay. Furthermore, the candidate target genes of miR-196a were analyzed by bioinformatics, and the target genes were validated by dual luciferase reporter assays, then the expression of target genes was detected by real-time quantitative polymerase chain reaction (RT-qPCR) and Western blot assays. The results showed that miR-196a promotes the proliferation and inhibits the apoptosis of immature Sertoli cells. miR-196a directly binds the 3 untranslated region (3 UTR) of RCC2 and ABCB9. The expression of miR-196a was shown to be negatively correlated with the messenger RNA and protein levels of the RCC2 and ABCB9 genes. The study demonstrates that miR-196a regulates immature Sertoli cell proliferation and apoptosis and inhibits the expression of RCC2 and ABCB9.

Examination of drug resistance activity of human TAP-like (ABCB9) expressed in yeast

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Authors: Ohashi-Kobayashi, A; Ohashi, K; Du, WB; Omote, H; Nakamoto, R; Al-shawi, M; Maeda, M

Abstract

A half-type ABC transporter, human TAP-like (hTAPL) tagged with histidine cluster, was expressed in budding yeast protease-deficient strain BJ5457, and the effect of expression for resistance to peptide compounds including antibiotics and proteinase inhibitor was examined. Among these Compounds, the yeast expressing hTAPL exhibits high sensitivity to valinomycin, a monovalent cation ionophore. A mutation in Walker A motif, which lost ATP-binding activity of hTAPL, eliminated the enhanced sensitivity to valinomycin. These findings suggest that the transport activity of hTAPL is important for conferring high valinomycin-sensitive phenotype to yeast. (c) 2006 Elsevier Inc. All rights reserved.