Rabbit HSP70 Polyclonal Antibody | anti-HSP70 antibody

HSP70 Antibody

Cat. Num. AAA9435445

• Gene Names: HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunocytochemistry, Immunohistochemistry
• Purity: Peptide affinity purified
• Synonyms: HSP70; Polyclonal Antibody; HSP70 Antibody; DnaK type molecular chaperone HSP70 1 antibody; Epididymis secretory protein Li 103 antibody; FLJ54303 antibody; FLJ54370 antibody; FLJ54392 antibody; FLJ54408 antibody; FLJ75127 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; anti-HSP70 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Purity/Purification: Peptide affinity purified
• Form/Format: 1*TBS (pH7.4), 1% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

• Applicable Applications for anti-HSP70 antibody: Western Blot (WB), Immunocytochemistry (ICC), Immunohistochemistry (IHC)
• Application Notes: WB: 1:500; IHC: 1:200; ICC: 1:200
• Immunogen: Peptide
• Conjugation: Unconjugated
• Preparation and Storage: Store at -20 degree C.

Western Blot (WB)

(Western blot analysis of HSP70 on different cell lysates using anti-HSP70 antibody at 1/500 dilution. Positive control: Lane 1: A549 Lane 2: MCF-7 Lane 3: HCT116)

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded human breast cancer tissue using anti-HSP70 antibody. Counter stained with hematoxylin.)

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded mouse testis tissue using anti-HSP70 antibody. Counter stained with hematoxylin.)

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded mouse brain tissue using anti-HSP70 antibody. Counter stained with hematoxylin.)

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded mouse prostate tissue using anti-HSP70 antibody. Counter stained with hematoxylin.)

Immunocytochemistry (ICC)

(ICC staining HSP70 in SHG-44 cells (green). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.)

Immunocytochemistry (ICC)

(ICC staining HSP70 in A431 cells (green). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.)

Immunocytochemistry (ICC)

(ICC staining HSP70 in SKBR-3 cells (green). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.)

Related Product Information for anti-HSP70 antibody

The 70 kilodalton heat shock proteins (Hsp70s) are a family of conserved ubiquitously expressedheat shock proteins. Proteins with similar structure exist in virtually all living organisms. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. When not interacting with a substrate peptide, Hsp70 is usually in an ATP bound state. Hsp70 by itself is characterized by a very weak ATPase activity, such that spontaneous hydrolysis will not occur for many minutes. As newly synthesized proteins emerge from theribosomes, the substrate binding domain of Hsp70 recognizes sequences of hydrophobic amino acid residues, and interacts with them. This spontaneous interaction is reversible, and in the ATP bound state Hsp70 may relatively freely bind and release peptides. However, the presence of a peptide in the binding domain stimulates the ATPase activity of Hsp70, increasing its normally slow rate of ATP hydrolysis.

Product Categories/Family for anti-HSP70 antibody

Total protein Ab

NCBI and Uniprot Product Information

• NCBI GI #: 194248072
• NCBI GeneID: 3303
• NCBI Accession #: NP_005336.3
• NCBI GenBank Nucleotide #: NM_005345.5
• UniProt Accession #: P0DMV8; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0; B4E3B6; P08107
• Molecular Weight: 70,052 Da
• NCBI Official Full Name: heat shock 70 kDa protein 1A/1B
• NCBI Official Synonym Full Names: heat shock 70kDa protein 1A
• NCBI Official Symbol: HSPA1A
• NCBI Official Synonym Symbols: HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A
• NCBI Protein Information: heat shock 70 kDa protein 1A/1B; HSP70-1/HSP70-2; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70 kDa protein 1/2; dnaK-type molecular chaperone HSP70-1
• UniProt Protein Name: Heat shock 70 kDa protein 1A
• Protein Family: HSP70 co-chaperone
• UniProt Gene Name: HSPA1A
• UniProt Synonym Gene Names: HSP721 PublicationManual assertion based on opinion iniRef.41; HSP70-12 PublicationsManual assertion based on opinion iniRef.4; HSP70.1

NCBI Description

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]

Uniprot Description

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).