Hsp70 1A Antibody (YA727)

Cat. No.: HY-P80712: Data Sheet COA
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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.

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10 μL	In-stock	Estimated Time of Arrival: December 31
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Hsp70 1A Antibody (YA727) Featured Recommendations:

1 Publications Citing Use of MCE Hsp70 1A Antibody (YA727)

•J Food Biochem. 2025 Jan 27.

WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Verification Image
Background
Documentation

Description

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

Host

Mouse

Clonality

Monoclonal

Molecular Weight

Predicted band size: 70 kDa;

Observed band size: 70 kDa

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.

Species Reactivity

Human, Mouse, Rat

SwissProt ID

P0DMV8

Gene ID

15511 [NCBI]

Immunogen

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

Application &
Dilution Ratio

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

Sensitivity	Endogenous	Purity	affinity purified
Conjugation	Non-conjugated	Modification	Unmodified
Isotype	IgG1

Appearance

Liquid

Formulation

Supplied in 1*PBS (pH 7.3), 50% glycerol and 0.5% BSA. Preservative: 0.02% sodium azide.

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

Shipping

Shipping with blue ice.

Verification Image

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.

Background

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:24318877, PubMed:26865365). 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). Required as a co-chaperone for optimal STUB1/CHIP ubiquitination of NFATC3 (By similarity). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). 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 (PubMed:28842558); (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell

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).

RRID

AB_3102168

Database

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

Research Field

Signal Transduction

Synonyms

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

Documentation

Select Batch:

Data Sheet (235 KB) SDS (251 KB)

COA (205 KB)

User Guide for Antibodies (1077 KB)

Hsp70 1A Antibody (YA727) Related Classifications

Help & FAQs

Do most proteins show cross-species activity?
Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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Hsp70 1A Antibody (YA727)

Hsp70 1A Antibody (YA727) Featured Recommendations:

1 Publications Citing Use of MCE Hsp70 1A Antibody (YA727)

Product Detail

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Background

Documentation

Hsp70 1A Antibody (YA727) Related Classifications

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