Rabbit Hsp70 Monoclonal Antibody | anti-Hspa1b antibody

Hsp70 Rabbit mAb

Cat. Num. AAA4752814

• Gene Names: Hspa1b; Hsp70; hsp68; Hsp70-1; Hsp70.1
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry, Immunocytochemistry, Immunofluorescence, Immunoprecipitation
• Purity: Affinity purified
• Synonyms: Hsp70; Monoclonal Antibody; Hsp70 Rabbit mAb; Heat shock 70kDa protein 1B; hsp68; HSP70B1; Hsp70-1; Hsp70.1; anti-Hspa1b antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Monoclonal
• Isotype: Rabbit IgG
• Clone Number: R07-6E9
• Specificity: Testis-specific. Gene expression databases
• Purity/Purification: Affinity purified
• Form/Format: Supplied in 50nM Tris-Glycine (pH7.4), 0.15M Nacl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

• Applicable Applications for anti-Hspa1b antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP)
• Application Notes: WB: 1:1000; IHC: 1:200; ICC/IF: 1:20; IP: 1:50
• Immunogen: Recombinant protein of mouse Hsp70
• Conjugation: Unconjugated
• Modification: Unmodification
• Preparation and Storage: Store at 4 degree C short term. Aliquot and store at -20 degree C long term. Avoid freeze/thaw cycle.

Western Blot (WB)

(Western blot detection of Hsp70 in K562,Rat Brain,3T3,Hela cell lysates using Hsp70 Rabbit mAb(1:1000 diluted). Predicted band size:70kDa. Observed band size:70kDa.)

Related Product Information for anti-Hspa1b antibody

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. 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. 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. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.

NCBI and Uniprot Product Information

• NCBI GI #: 124339826
• NCBI GeneID: 15511
• NCBI Accession #: NP_034608.2
• NCBI GenBank Nucleotide #: NM_010478.2
• UniProt Accession #: P17879; Q61689; Q925V6
• Molecular Weight: 70,176 Da
• NCBI Official Full Name: heat shock 70 kDa protein 1B
• NCBI Official Synonym Full Names: heat shock protein 1B
• NCBI Official Symbol: Hspa1b
• NCBI Official Synonym Symbols: Hsp70; hsp68; Hsp70-1; Hsp70.1
• NCBI Protein Information: heat shock 70 kDa protein 1B; heat shock protein 70.1; 68 kDa heat shock protein; heat shock 70kDa protein 1B; heat shock protein, 70 kDa 1
• UniProt Protein Name: Heat shock 70 kDa protein 1B
• Protein Family: HSP70 co-chaperone
• UniProt Gene Name: Hspa1b
• UniProt Synonym Gene Names: Hcp70.1; Hsp70-1; Hsp70a1; Hspa1; HSP70.1
• UniProt Entry Name: HS71B_MOUSE

Uniprot Description

HSP70: a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70.

Protein type: Motility/polarity/chemotaxis; Chaperone; Heat shock protein

Cellular Component: signalosome; focal adhesion; protein complex; mitochondrion; basolateral plasma membrane; inclusion body; cytosol; ribonucleoprotein complex; centriole; perinuclear region of cytoplasm; cytoplasm; apical plasma membrane; nuclear speck; nucleus; vesicle; ubiquitin ligase complex

Molecular Function: NF-kappaB binding; enzyme binding; protease binding; G-protein-coupled receptor binding; ubiquitin protein ligase binding; heat shock protein binding; ATPase activity; unfolded protein binding; double-stranded RNA binding; protein N-terminus binding; ATPase activity, coupled; ATP binding

Biological Process: protein folding; response to heat; DNA repair; telomere maintenance