功能Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones.
序列相似性Belongs to the heat shock protein 70 family.
结构域The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain.
翻译后修饰Phosphorylated upon DNA damage, probably by ATM or ATR. ISGylated.
细胞定位Cytoplasm. Melanosome. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Epididymis secretory sperm binding protein Li 72p antibody
Heat shock 70 kDa protein 8 antibody
Heat shock 70kD protein 10 antibody
Heat shock 70kD protein 8 antibody
Heat shock 70kDa protein 8 antibody
Heat shock cognate 71 kDa protein antibody
Heat shock cognate protein 54 antibody
Heat shock cognate protein 71 kDa antibody
Heat shock protein 8 antibody
Heat shock protein A8 antibody
Heat-shock70-KD protein 10, formerly antibody
HEL 33 antibody
HEL S 72p antibody
Lipopolysaccharide associated protein 1 antibody
LPS associated protein 1 antibody
LPS associated protein antibody
N-myristoyltransferase inhibitor protein 71 antibody
Anti-Hsc70 antibody 图像
Western blot - Hsc70 antibody (ab79857)
All lanes : Anti-Hsc70 antibody (ab79857) at 1/100 dilution
Lane 1 : Extract prepared from whole salmon Lane 2 : Extract prepared from whole salmon
Lysates/proteins at 10 µg per lane.
Secondary HRP-conjugated goat anti rabbit IgG
Predicted band size : 71 kDa
Anti-Hsc70 antibody (ab79857)参考文献
This product has been referenced in:
Rengarajan C et al. Endocytosis of Fgf8 is a double-stage process and regulates spreading and signaling. PLoS One9:e86373 (2014).
Read more (PubMed: 24466061) »
Vickers TA & Crooke ST Antisense oligonucleotides capable of promoting specific target mRNA reduction via competing RNase H1-dependent and independent mechanisms. PLoS One9:e108625 (2014).
Read more (PubMed: 25299183) »