Hsp70 1A Antibody (YA727)
(Synonyms: HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A.)Based on 1 publication(s) in Google Scholar
Hsp70 1A Antibody (YA727) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Hsp70 1A.
-
Host:
Mouse
-
Isotype:
IgG
-
Application:
WB, IHC-F, IHC-P, ICC/IF
-
Reactivity :
Human, Mouse, Rat
-
Formulation:
Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.
-
Conjugation:
Non-conjugated
Publications Citing Use of MedChemExpress (MCE) Hsp70 1A Antibody (YA727)
More
Applications
| Application |
WB
WB: Western Blot
|
IHC-P
IHC-P: Immunohistochemistry-Paraffin
|
IHC-F
IHC-F: Immunohistochemistry-Frozen
|
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:50-1:100 | 1:50-1:200 |
Product Details
Hsp70 1A Antibody (YA727) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Hsp70 1A.
-
Host Mouse
-
Clonality Monoclonal
-
Species ReactivityHuman, Mouse, Rat
-
Observed Molecular WeightObserved band size: 70 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
-
Calculated Molecular Weight Predicted band size: 70 kDa
Entrez Gene: 15511 Human ; 3303 Human ; 193740 Mouse ; 3304 Mouse ; 24472 Rat 294254
SwissProt: P0DMV8 Human ; P0DMV9 Human ; P17879 Mouse ; Q61696 Mouse ; P0DMW0 Rat P0DMW1
OMIM: 140550 Human
Synthetic peptide corresponding to HSP70.The exact sequence is proprietary to MCE.
Endogenous
affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
-
Appearance
Solution
-
Formulation
Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.
-
Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
-
Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
-
Shipping
Shipping with blue ice.
Publications (1)
-
Journal Impact Factor
-
Most Recent
Verification Images
-
Western blot analysis of extracts from Hela (lane 1) and 293T (lane 2) and Jurkat (lane 3) and NIH3T3 (lane 4) using Hsp70 1A antibody. Proteins were transferred to a PVDF membrane and blocked with 5% nonfat powdered milk in PBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (GAPDH, 1/3000) was diluted with 5% nonfat powdered milk in PBST at 4°C overnight. Goat Anti-mouse IgG-HRP Secondary Antibody (1/8,000) was incubated for 45min at room temperature. -
Immunocytochemistry analysis of Hela cells labeling Hsp70 1A with Hsp70 1A Antibody (HY-P80712) at 1/100 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes at room temperature, then blocked with quick block buffer for 10 minutes at room temperature. Cells were then incubated with Hsp70 1A Antibody (HY-P80712) at 1/100 dilution in quick block buffer overnight at 4 ℃.AF488-conjugated Goat Anti-Mouse IgG H&L (HY-P8005, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue).
-
Immunocytochemistry analysis of HepG2 cells labeling Hsp70 1A with Hsp70 1A Antibody (HY-P80712) at 1/100 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes at room temperature, then blocked with quick block buffer for 10 minutes at room temperature. Cells were then incubated with Hsp70 1A Antibody (HY-P80712) at 1/100 dilution in quick block buffer overnight at 4 ℃.AF488-conjugated Goat Anti-Mouse IgG H&L (HY-P8005, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue).
Background
-
Function
Hsp70 1A is a 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. Required as a co-chaperone for optimal STUB1/CHIP ubiquitination of NFATC3. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation; (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell[1][2][3][4][5][6][7][8][9].
-
Subcellular Localization
Cytoplasm; Nucleus; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Secreted
-
Expression
Induction:By heat shock -
Isoforms & Post-Translational Modification
P0DMV8 has 2 isomers: P0DMV8-1: 70052 Da (predicted); P0DMV8-2: 63937 Da (predicted).
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 -
Subunit
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:12853476, PubMed:15383005, PubMed:15963462, PubMed:17233114, PubMed:18620420, PubMed:21081504).
-
SwissProt ID
-
Synonyms
HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A.
-
Research Field
Signal Transduction
Documentation
-
Data Sheet (262 KB)
-
SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
-
User Guide for Antibodies (1077 KB)
References
[1]. Mayer MP, et al. Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem Sci. 2013 Oct;38(10):507-14. [Content Brief]
[2]. Rauch JN, et al. Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J Biol Chem. 2014 Jan 17;289(3):1402-14. [Content Brief]
[3]. Radons J, et al. The human HSP70 family of chaperones: where do we stand?. Cell Stress Chaperones. 2016 May;21(3):379-404. [Content Brief]
[4]. Seo JH, et al. ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation. Nat Commun. 2016 Oct 6;7:12882. [Content Brief]
[5]. Fang CT, et al. HSP70 regulates the function of mitotic centrosomes. Cell Mol Life Sci. 2016 Oct;73(20):3949-60. [Content Brief]
[6]. Shang Y, et al. Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1. Biochem Biophys Res Commun. 2014 Mar 28;446(1):387-92. [Content Brief]
[7]. Chen Z, et al. The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3. Immunity. 2013 Aug 22;39(2):272-85. [Content Brief]
[8]. Shi Y, et al. Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 1998 Mar 1;12(5):654-66. [Content Brief]
[9]. Wang WF, et al. HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells. Nat Commun. 2017 Aug 25;8(1):363. [Content Brief]