Hsp70(C-term) Antibody (YA5200)

Cat. No.: HY-P85508: Data Sheet User Guide for Antibodies
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Hsp70(C-term) Antibody (YA5200) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Hsp70(C-term).

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

Size		Stock
50 μL		Get quote
100 μL		Get quote

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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
Background
Documentation

Description

Hsp70(C-term) Antibody (YA5200) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Hsp70(C-term).

Host

Mouse

Clonality

Monoclonal

Molecular Weight

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

SwissProt ID

P0DMV8 / P0DMV9

Gene ID

3303 [NCBI]

Immunogen

Purified recombinant human Hsp70(C-terminus) protein fragments expressed in E.coli.

Application &
Dilution Ratio

Application	Dilution Ratio
WB WB: Western Blot	1:1000

Purity	affinity chromatography.	Conjugation	Non-conjugated
Modification	Unmodified

Appearance

Liquid

Formulation

Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Storage & Stability

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

Shipping

Shipping with blue ice.

Background

Function：P0DMV8: 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.
P0DMV9: 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).

Subcellular Localization：P0DMV8: Cytoplasm; Nucleus; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Secreted
P0DMV9: Cytoplasm; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Expression：
Tissue_specificity: P0DMV9: HSPA1B is testis-specific
Induction: P0DMV8: By heat shock
P0DMV9: 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：P0DMV8: 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).
P0DMV9: May be an auxiliary component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661).

Synonyms

DAQB 147D11.1 001; 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; heat shock protein 70; HSP70 1; HSP70 2; HSP70-1/HSP70-2; HSP70-1A; HSP70.1; HSP70.1/HSP70.2; HSP70I; HSP71_HUMAN; HSP72; HSPA1; HSPA1A; HSPA1B; XXbac BCX40G17.3 001.

Documentation

User Guide for Antibodies (1077 KB)