Rabbit Hsp70 Monoclonal Antibody | anti-Hs antibody

Hsp70 Rabbit Monoclonal Antibody

Cat. Num. AAA3014033

• Gene Names: HSPA1B; HSP72; HSPA1; HSX70; HSP70-1; HSP70-2; HSP70.1; HSP70.2; HSP70-1B
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Flow Cytometry, Functional Assay
• Purity: Protein A affinity purified
• Synonyms: Hsp70; Monoclonal Antibody; Hsp70 Rabbit Monoclonal Antibody; Heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2; HSPA1A; HSPA1; HSX70; HSPA1B; HSP-70; HSP 70; anti-Hs antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Monoclonal
• Isotype: IgG
• Specificity: This antibody detects endogenous levels of Hsp70 and does not cross-react with related proteins.
• Purity/Purification: Protein A affinity purified
• Form/Format: Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
• Sequence Length: 641

• Applicable Applications for anti-Hs antibody: Western Blot (WB), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Flow Cytometry (FC/FACS)
• Application Notes: WB: 1:1000-1:5000; IHC: 1:50-1:200; ICC: 1:50-1:200; IF: 1:50-1:200; FC/FACS: 1:10-1:100
• Immunogen: Recombinant antibody.
• Preparation and Storage: Store at 4 degree C short term.; Aliquot and store at -20 degree C long term.; Avoid freeze-thaw cycles.

Western Blot (WB)

(Western Blot (WB) analysis of Hsp70 Rabbit mAb at 1:1000 dilutionLane1:MCF-7 whole cell lysateLane2:HCT116 whole cell lysate)

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using anti-Hsp70 antibody. Counter stained with hematoxylin.)

Immunocytochemistry (ICC)

(ICC staining Hsp70 in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton *100/PBS.)

Flow Cytometry (FC/FACS)

(Flow cytometric analysis of Hela cells with Hsp70 antibody at 1/50 dilution (blue) compared with an unlabelled control (cells without incubation with primary antibody; red). Alexa Fluor 488-conjugated goat anti rabbit IgG was used as the secondary antibody.)

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 MCF-7 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton *100/PBS.)

Related Product Information for anti-Hs antibody

The HSP 70 family is composed of four highly conserved proteins: HSP 70, HSC 70, GRP 75 and GRP 78. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70 play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery and are found in both the cytosol and nucleus of mammalian cells. GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains. GRP 75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. It has been postulated that members of the HSP 70 family act as force-generating motors, relying on the hydrolysis of ATP for their activity

NCBI and Uniprot Product Information

• NCBI GI #: 167466173
• NCBI GeneID: 3304
• NCBI Accession #: NP_005337.2
• NCBI GenBank Nucleotide #: NP_005337.2
• UniProt Accession #: P0DMV9; P0DMV8
• Molecular Weight: ~ 70kDa
• NCBI Official Full Name: heat shock 70 kDa protein 1B
• NCBI Official Synonym Full Names: heat shock protein family A (Hsp70) member 1B
• NCBI Official Symbol: HSPA1B
• NCBI Official Synonym Symbols: HSP72; HSPA1; HSX70; HSP70-1; HSP70-2; HSP70.1; HSP70.2; HSP70-1B
• NCBI Protein Information: heat shock 70 kDa protein 1B
• UniProt Protein Name: Heat shock 70 kDa protein 1B
• Protein Family: HSP70 co-chaperone
• UniProt Gene Name: HSPA1B
• UniProt Synonym Gene Names: HSP721 PublicationManual assertion based on opinion iniRef.36; HSP70-22 PublicationsManual assertion based on opinion iniRef.3; HSP70.2

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).