dnaK Antibody (OABB00225)

Catalog No: OABB00225

Size:100UG

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Lane 1: Mouse Brain Tissue Lysate
Lane 2: MouseTesticleTissue Lysate

IHC(P): Rat brain Tissue

Product Info

• Tested Species Reactivity: Human, Mouse, Rat
• Predicted Species Reactivity: Hamster|Human|Mouse|Rat
• Product Format: Lyophilized. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
• Clonality: Polyclonal
• Clone: Polyclonal
• Isotype: Rabbit IgG
• Application: Flow cytometry|Immunocytochemistry|Immunofluorescence|Immunohistochemistry|Immunohistochemistry-Frozen|Western blot
• Additional Information: Notes: Tested Species: In-house tested species with positive results.
  Predicted Species: Species predicted to be fit for the product based on sequence similarities.
  By Heat: Boiling the paraffin sections in 10mM citrate buffer, pH6.0, for 20mins is required for the staining of formalin/paraffin sections.
  Other applications have not been tested.
  Optimal dilutions should be determined by end users.
  
  Background: 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.
  Background: 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.1,2 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.3
• Reconstitution and Storage: 2°C to 8°C|-20°C
• Immunogen: Polypeptide
• Purification: Affinity Purified
• Predicted Homology Based on Immunogen Sequence: Human; Mouse; Rat
• Concentration: 500 ug/ml
• Specificity: No cross reactivity with other proteins.
• Application Info: Western blot: 0.1-0.5 ug/ml: Human, Mouse, Rat
  Immunohistochemistry (Paraffin-embedded Section): 0.5-1 ug/ml: Human, Mouse, Rat: By Heat
  Immunohistochemistry (Frozen Section): 0.5-1 ug/ml: Mouse, Rat
  Immunocytochemistry : 0.5-1 ug/ml: Human
  Immunocytochemistry/Immunofluorescence: 2 ug/ml: Human
  Flow Cytometry: 1-3 ug/1x10^6 cells: Human
• Reference: 1. Tavaria M, Gabriele T, Kola I, Anderson RL (April 1996). "A hitchhiker's guide to the human Hsp70
  family". Cell Stress Chaperones 1 (1): 23–8.
  2. Morano KA (October 2007). "New tricks for an old dog: the evolving world of Hsp70". Ann. N. Y.
  Acad. Sci. 1113: 1–14.
  3. Luders, J.; Demand, J.; Hohfeld, J. (2000), Journal of Biological Chemistry 275 (7): 4613–461,
  //www.jbc.org/cgi/content/full/275/7/4613, retrieved on 2009-04-07
• Storage Buffer: Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
• Description: Rabbit IgG polyclonal antibody for Heat shock 70 kDa protein 1A/1B(HSPA1A/HSPA1B) detection. Tested with WB, IHC-P, IHC-F, ICC, ICC/IF, FCM in Human;Mouse;Rat.

Target Info

• Gene Symbol: HSPA1A|HSPA1B
• Gene Full Name: heat shock protein family A (Hsp70) member 1A|heat shock protein family A (Hsp70) member 1B
• Alias Symbols: dnaK-type molecular chaperone HSP70-1;epididymis secretory protein Li 103;epididymis secretory sperm binding protein;heat shock 70 kDa protein 1;heat shock 70 kDa protein 1/2;heat shock 70 kDa protein 1A;heat shock 70 kDa protein 1A/1B;Heat shock 70 kDa protein 1B;Heat shock 70 kDa protein 2;heat shock 70kD protein 1A;heat shock 70kD protein 1B;heat shock 70kDa protein 1A;heat shock 70kDa protein 1B;heat shock-induced protein;HEL-S-103;HSP70.1;HSP70.1/HSP70.2;HSP70.2;HSP70-1;HSP70-1/HSP70-2;HSP70-1A;HSP70-1B;HSP70-2;HSP70I;HSP72;HSPA1;HSX70.
• NCBI Gene Id: 3303|3304
• Protein Name: Heat shock 70 kDa protein 1A|Heat shock 70 kDa protein 1B
• Description of Target: 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).|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).
• Uniprot ID: P0DMV8|P0DMV9
• Protein Accession #: NP_820282.1; WP_005770882.1
• Nucleotide Accession #: NC_002971.3