HSP70, Polyclonal Antibody

Rabbit Anti-Human HSP70 Acetyl Lys77 Polyclonal; HSP70 Acetylated lysine 77 Antibody; HSP70 acLys77 Antibody; HSP70 acK77 Antibody; Acetylated Lysine HSP70 Antibody; HSP70 AcetylLys77 Antibody; HSP70 AceyltK77 Antibody; DnaK type molecular chaperone HSP70 1 antibody; Epididymis secretory protein Li 103 antibody; Heat shock 70 kDa protein 1 antibody; Heat shock 70 kDa protein 1/2 antibody; Heat shock 70 kDa protein 1A/1B antibody; Heat shock 70kDa protein 1A antibody; Heat shock 70kDa protein 1B antibody; Heat shock induced protein antibody; HEL S 103 antibody; HSP70 1 antibody; HSP70 1B antibody; HSP70 2 antibody; HSP70-1/HSP70-2 antibody; HSP70-1A antibody; HSP70.1 antibody; HSP70.1/HSP70.2 antibody; HSP70I antibody; HSP71_HUMAN antibody; HSP72 antibody; HSPA1 antibody; HSPA1A antibody; HSPA1B antibody

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit

Binds to acetylated lysine 77 on HSP70. Detects 70 kDa band.

Peptide Affinity Purified

Store at -20 degree C.

Small volumes of anti-HSP70 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5).
All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.

Antibodies; Cancer; Heat Shock; Cell Signaling; Protein Trafficking; Chaperone Proteins; Cancer; Tumor Biomarkers

Western Blot (WB), ELISA (EIA), Immunocytochemistry (ICC), Immunofluorescence (IF)

WB: 1:1000
ELISA: 1:1000
ICC/IF: 1:60

Immunocytochemistry/Immunofluorescence analysis using Rabbit Anti-HSP70 Acetyl Lys77 Polyclonal Antibody (SPC-743). Tissue: Embryonic kidney cells (HEK293) cultured overnight with 50 uM H2O2. Species: Human. Fixation: 5% Formaldehyde for 5 min. Primary Antibody: Rabbit Anti-HSP70 Acetyl Lys77 Polyclonal Antibody (SPC-743) at 1:60 for 30-60 min at RT. Secondary Antibody: Goat Anti-Mouse Alexa Fluor 488 at 1:1500 for 30-60 min at RT. Counterstain: Phalloidin Alexa Fluor 633 F-Actin stain; DAPI (blue) nuclear stain at 1:250, 1:50000 for 30-60 min at RT. Localization: Cytoplasmic. Magnification: 20X (2X Zoom). (A) DAPI (blue) nuclear stain. (B) Phalloidin Alex Fluor 633 F-Actin stain. (C) HSP70 Antibody (Acetyl Lys77). (D) Composite. Courtesy of: Dr. Robert Burke, University of Victoria.

Western blot analysis of Human Cervical cancer cell line (HeLa) lysate showing detection of ~70 kDa HSP70 Acetyl Lys77 protein using Rabbit Anti-HSP70 Acetyl Lys77 Polyclonal Antibody (SPC-743). Lane 1: Molecular Weight Ladder (MW). Lane 2: Cervical Cancer cell line (HeLa) lysate. Lane 3: H2O2 Cervical Cancer cell line (HeLa) lysate. Load: 10 ug. Block: 5% Skim Milk in 1X TBST. Primary Antibody: Rabbit Anti-HSP70 Acetyl Lys77 Polyclonal Antibody (SPC-743) at 1:1000 for 2 hours at RT. Secondary Antibody: Goat Anti-Rabbit HRP:IgG at 1:3000 for 1 hour at RT. Color Development: ECL solution for 5 min at RT. Predicted/Observed Size: ~70 kDa.

63,937 Da

heat shock protein family A (Hsp70) member 1A

heat shock 70 kDa protein 1A

Heat shock 70 kDa protein 1A

; HSP70.1  [Similar Products]

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).

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