Anti-Hsp70/HSPA1A/HSPA1B Antibody Picoband®

Primary Antibodies

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

85497 MW

Western blot, 0.1-0.5?g/ml, Human, Mouse, Rat

Immunohistochemistry (Paraffin-embedded Section), 0.5-1?g/ml, Human, Mouse, Rat, By Heat

Immunohistochemistry (Frozen Section), 0.5-1?g/ml, Mouse, Rat

Immunocytochemistry , 0.5-1?g/ml, Human

Immunocytochemistry/Immunofluorescence, 2?g/ml, Human

Flow Cytometry (Fixed), 1-3?g/1x10⁶ cells, Human

heat shock protein family A (Hsp70) member 1A/1B

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.

Each vial contains 5 mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05 mg Thimerosal, 0.05 mg NaN3.

Add 0.2 ml of distilled water will yield a concentration of 500 ug/ml.

Cancer, Chaperones, Heat Shock Proteins, Protein Trafficking, Signal Transduction, Tumor Biomarkers

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).

Boster Bio Anti-Hsp70/HSPA1A/HSPA1B Antibody catalog # PA1214. Tested in Flow Cytometry, IF, IHC, IHC-F, ICC, WB applications. This antibody reacts with Human, Mouse, Rat.

Belongs to the beta-catenin family.