Anti-Hsp70/HSPA1A/HSPA1B Antibody Picoband® Fluoro594 Conjugated

The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. All of the Hsp70 proteins have three major functional domains: An N-terminal ATPase domain binds ATP (Adenosine triphosphate) and hydrolyzes it to ADP (Adenosine diphosphate) ; A substrate binding domain contains a groove with an affinity for neutral, hydrophobic amino acid residues; A C-terminal domain rich in alpha helical structure acts as a 'lid' for the substrate binding domain. By binding tightly to partially-synthesized peptide sequences (incomplete proteins), Hsp70 prevents them from aggregating and being rendered nonfunctional. And it also can act to protect cells from thermal or oxidative stress. Finally, Hsp70 seems to be able to participate in disposal of damaged or defective proteins. Interaction with CHIP (Carboxyl-terminus of Hsp70 Interacting Protein) – an E3 ubiquitin ligase– allows Hsp70 to pass proteins to the cell's ubiquitination and proteolysis pathways.

Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level) . .

Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22647378, PubMed:22699938, PubMed:22155184) . Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity) . .

1. Tavaria M, Gabriele T, Kola I, Anderson RL (April 1996) . A hitchhiker's guide to the human Hsp70 family. Cell Stress Chaperones 1 (1) : 23–8. 2. Morano KA (October 2007) . New tricks for an old dog: the evolving world of Hsp70. Ann. N. Y. Acad. Sci. 1113: 1–14. 3. Luders, J.; Demand, J.; Hohfeld, J. (2000), Journal of Biological Chemistry 275 (7) : 4613–461, http://www.jbc.org/cgi/content/full/275/7/4613, retrieved on 2009-04-07

Cytoplasm. Nucleus . Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell junction. Cell membrane . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity) . Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation) . Interaction with GLIS2 and MUC1 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization. The majority of beta-catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. .