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anti-HSP70 antibody :: Rabbit HSP70 Polyclonal Antibody

Scan QR to view Datasheet Catalog #    MBS9606746
Western Blot (WB)
Unit / Price
0.1 mL  /  $255 +1 FREE 8GB USB
0.2 mL  /  $295 +1 FREE 8GB USB
 
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 Product Name   

HSP70, Polyclonal Antibody

★Popular Item★
 Also Known As   

HSP70 Antibody

 Product Synonym Names    DnaK type molecular chaperone HSP70 1; Epididymis secretory protein Li 103; FLJ54303; FLJ54370; FLJ54392; FLJ54408; FLJ75127; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A/1B; Heat shock 70kDa protein 1A; Heat shock 70kDa protein 1B; Heat shock induced protein; HEL S 103; HSP70 1; HSP70 1B; HSP70 2; HSP70-1/HSP70-2; HSP70-1A; HSP70.1; HSP70.1/HSP70.2; HSP70I; HSP71_HUMAN; HSP72; HSPA1; HSPA1A; HSPA1B
 Product Gene Name   

anti-HSP70 antibody

[Similar Products]
 Product Synonym Gene Name    HSPA1A [Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 3D Structure    ModBase 3D Structure for P0DMV8
 Clonality    Polyclonal
 Isotype    IgG
 Host    Rabbit
 Species Reactivity    Human, Mouse, Rat
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 Specificity    HSP70 antibody detects endogenous levels of total HSP70
 Purity/Purification    The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin.
 Form/Format    Liquid
Phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
 Concentration    1mg/ml (lot specific)
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 Immunogen    N term-peptide of human HSP70
 Subcellular Location    Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
 Tissue Specificity    By heat shock.
 Conjugation    Unconjugated
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 Preparation and Storage    Store at -20 degree C. Stable for 12 months from date of receipt.
 Other Notes    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.
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Related Product Information for anti-HSP70 antibody

   Description: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP-and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2, 3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1, 4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1, 3). They also play a role in vesicle formation and protein trafficking (2).
Function: 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).
Subunit Structure: Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (PubMed:21081504, PubMed:12853476, PubMed:18620420, PubMed:17233114, PubMed:15383005, PubMed:15963462). Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed (PubMed:11274138). Interacts with TRIM5 (via B30.2/SPRY domain) (PubMed:20053985). Interacts with METTL21A (PubMed:23921388). Interacts with DNAAF2 (By similarity). Interacts with PRKN (PubMed:24270810). Interacts with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction enhances NOD2 stability (PubMed:24790089). Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes (PubMed:22528486). Interacts with RNF207 (via the C-terminus); this interaction additively increases KCNH2 expression (PubMed:25281747). Interacts with HSF1 (via transactivation domain); this interaction results in the inhibition of heat shock-and HSF1-induced transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:7935376, PubMed:9499401). Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form interact with HOPX and STUB1 respectively (PubMed:27708256). Interacts with NEDD1 (PubMed:27137183). Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105 (PubMed:24318877). Interacts with SMAD3 (PubMed:24613385). Interacts with DNAJC8 (PubMed:27133716).
Post-translational Modifications: In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress.
Similarity: The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. Belongs to the heat shock protein 70 family.
 Applications Tested/Suitable for anti-HSP70 antibody   

Western Blot (WB), ELISA (EIA)

 Application Notes for anti-HSP70 antibody    WB: 1:500-1:2000
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 Western Blot (WB) of anti-HSP70 antibody    Western blot analysis of Hela whole cell lysates, using HSP70 Antibody. The lane on the left is treated with the antigen-specific peptide.
anti-HSP70 antibody Western Blot (WB) (WB) image
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NCBI/Uniprot data below describe general gene information for HSP70. It may not necessarily be applicable to this product.
 NCBI GI #    194248072
 NCBI GeneID    3303
 NCBI Accession #    NP_005336.3 [Other Products]
 NCBI GenBank Nucleotide #    NM_005345.5 [Other Products]
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 UniProt Primary Accession #    P0DMV8 [Other Products]
 UniProt Secondary Accession #    P08107; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0; B4E3B6 [Other Products]
 UniProt Related Accession #    P0DMV8 [Other Products]
 Molecular Weight    Observed: 70 kDa
Predicted: 71 kDa
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 NCBI Official Full Name    heat shock 70 kDa protein 1A
 NCBI Official Synonym Full Names    heat shock protein family A (Hsp70) member 1A
 NCBI Official Symbol    HSPA1A [Similar Products]
 NCBI Official Synonym Symbols   
HSP72; HSPA1; HSP70I; HSP70-1; HSP70-2; HSP70.1; HSP70.2; HSP70-1A; HEL-S-103
[Similar Products]
 NCBI Protein Information    heat shock 70 kDa protein 1A
 UniProt Protein Name    Heat shock 70 kDa protein 1A
 UniProt Synonym Protein Names   
Heat shock 70 kDa protein 1; HSP70-12 PublicationsManual assertion based on opinion iniRef.4"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-110, ALTERNATIVE SPLICING (ISOFORM 1).
 Protein Family    HSP70 co-chaperone
 UniProt Gene Name    HSPA1A [Similar Products]
 UniProt Synonym Gene Names    HSP721 PublicationManual assertion based on opinion iniRef.41; HSP70-12 PublicationsManual assertion based on opinion iniRef.4; HSP70.1 [Similar Products]
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 NCBI Summary for HSP70    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]
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 UniProt Comments for HSP70    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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 Research Articles on HSP70    1. HSPA1A overexpression promotes lipid accumulation in hepatocytes.
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 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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Products associated with anti-HSP70 antibodyPathways associated with anti-HSP70 antibody
 Reference Product  PubMed Publications
 DNAJB1 antibody  >14 publications with HSP70 and DNAJB1
 HSF1 antibody  >11 publications with HSP70 and HSF1
 STIP1 antibody  >3 publications with HSP70 and STIP1
 HSPBP1 antibody  >3 publications with HSP70 and HSPBP1
 TP53 antibody  >2 publications with HSP70 and TP53
 BAG3 antibody  >2 publications with HSP70 and BAG3
 STUB1 antibody  >1 publications with HSP70 and STUB1
 Products by Pathway  Pathway Diagram
 Antigen Processing And Presentation Pathway antibodies  Antigen Processing And Presentation Pathway Diagram
 Antigen Processing And Presentation Pathway antibodies  Antigen Processing And Presentation Pathway Diagram
 Apoptosis Modulation By HSP70 Pathway antibodies  Apoptosis Modulation By HSP70 Pathway Diagram
 Direct P53 Effectors Pathway antibodies  Direct P53 Effectors Pathway Diagram
 Endocytosis Pathway antibodies  Endocytosis Pathway Diagram
 Endocytosis Pathway antibodies  Endocytosis Pathway Diagram
 Epstein-Barr Virus Infection Pathway antibodies  Epstein-Barr Virus Infection Pathway Diagram
 Epstein-Barr Virus Infection Pathway antibodies  Epstein-Barr Virus Infection Pathway Diagram
 Estrogen Signaling Pathway antibodies  Estrogen Signaling Pathway Diagram
 Estrogen Signaling Pathway antibodies  Estrogen Signaling Pathway Diagram
Diseases associated with anti-HSP70 antibodyOrgans/Tissues associated with anti-HSP70 antibody
 Disease Name  Pubmed Publications
 Neoplasms Antibodies  >31 publications with HSP70 and Neoplasms
 Cardiovascular Diseases Antibodies  >21 publications with HSP70 and Cardiovascular Diseases
 Inflammation Antibodies  >19 publications with HSP70 and Inflammation
 Drug Toxicity Antibodies  >15 publications with HSP70 and Drug Toxicity
 Nervous System Diseases Antibodies  >12 publications with HSP70 and Nervous System Diseases
 Liver Diseases Antibodies  >9 publications with HSP70 and Liver Diseases
 Necrosis Antibodies  >8 publications with HSP70 and Necrosis
 Brain Diseases Antibodies  >8 publications with HSP70 and Brain Diseases
 Heart Diseases Antibodies  >8 publications with HSP70 and Heart Diseases
 Liver Neoplasms Antibodies  >6 publications with HSP70 and Liver Neoplasms
 Organ/Tissue Name  Pubmed Publications
 Blood Antibodies  >37 publications with HSP70 and Blood
 Liver Antibodies  >18 publications with HSP70 and Liver
 Brain Antibodies  >17 publications with HSP70 and Brain
 Vascular Antibodies  >11 publications with HSP70 and Vascular
 Heart Antibodies  >8 publications with HSP70 and Heart
 Kidney Antibodies  >8 publications with HSP70 and Kidney
 Nerve Antibodies  >8 publications with HSP70 and Nerve
 Muscle Antibodies  >8 publications with HSP70 and Muscle
 Skin Antibodies  >7 publications with HSP70 and Skin
 Lung Antibodies  >6 publications with HSP70 and Lung
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