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- Bioss
- bs-14368P
- 2025年10月16日
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- 规格：
500ug
| 产品编号 | bs-14368P |
| 英文名称 | DNAJA4 Antibody Blocking Peptide |
| 中文名称 | DNAJA4蛋白封闭多肽 |
| 英文别名 | DnaJ (Hsp40) homolog subfamily A member 4; DnaJ (Hsp40) homolog, subfamily A, member4; DNAJ A4; DnaJ homolog subfamily A member 4; DNAJA 4; DNAJA4; DNJA4_HUMAN; MST104; MSTP104; PRO1472. |
| 纯化方法 | HPLC |
| 研究领域 | Cardiovascular > Lipids / Lipoproteins > Lipid Metabolism > Cholesterol Metabolism Metabolism > Pathways and Processes > Metabolic signaling pathways > Lipid and lipoprotein metabolism > Cholesterol Metabolism Signal Transduction > Metabolism > Lipid metabolism Signal Transduction > Protein Trafficking > Chaperones > Heat Shock Proteins Signal Transduction > Protein Trafficking > Chaperones > Other Chaperones |
| 亚细胞定位 | Membrane. |
| 相似性 | Contains 1 CR-type zinc finger. Contains 1 J domain. |
| 保存条件 | Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
| 注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| 背景资料 | The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJA4 (DnaJ homolog subfamily A member 4) is a SREBP-regulated chaperone that is thought to regulate the cholesterol biosynthesis pathway. |
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DNAJA4 Antibody Blocking Peptide(bs-14368P)-500ug
￥880
