Hsp70 1A Antibody (YA727)

(Synonyms: HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A.)
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Hsp70 1A Antibody (YA727) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Hsp70 1A.

For research use only. We do not sell to patients.
  • 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)

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Applications

Application
WB Info
WB: Western Blot
IHC-P Info
IHC-P: Immunohistochemistry-Paraffin
IHC-F Info
IHC-F: Immunohistochemistry-Frozen
ICC/IF Info
ICC/IF: Immunocytochemistry/
Immunofluorescence
Dilution Ratio 1:500-1:1000 1:50-1:100 1:50-1:100 1:50-1:200

Product Details

Description

Hsp70 1A Antibody (YA727) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Hsp70 1A.

  • Host Mouse
  • Clonality Monoclonal
  • Species Reactivity
    Human, Mouse, Rat
  • Observed Molecular Weight
    Observed band size: 70 kDa Info
    Note: 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
Immunogen

Synthetic peptide corresponding to HSP70.The exact sequence is proprietary to MCE.

Sensitivity

Endogenous

Purification

affinity purified

Conjugation

Non-conjugated

Modification

Unmodified

Isotype

IgG

RRID

AB_3102168

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.

Verification Images

  • Experimental Validation Results for Hsp70 1A Antibody (YA727)
    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.
  • Experimental Validation Results for Hsp70 1A Antibody (YA727)
    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).
  • Experimental Validation Results for Hsp70 1A Antibody (YA727)
    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

    P0DMV8

  • Gene ID
  • Synonyms

    HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A.

  • Research Field

    Signal Transduction

References

Hsp70 1A Antibody (YA727) Related Classifications

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100 mg

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