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Antibodies
Anti-Hsp70 Antibody
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产品名称:
Anti-Hsp70 Antibody
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简单介绍
Anti-Hsp70
Antibody
Anti-Hsp70 Antibody
的详细介绍
Overview
Name:
Anti-Hsp70
Antibody
See all Hsp70 primary antibodies
Description:
Rabbit monoclonal antibody to Hsp70
Specificity:
This antibody detects endogenous levels of Hsp70 and does not cross-react with related proteins.
Applications:
WB, ICC/IF, IHC, FC
Reactivity:
Human, Mouse, Rat
Immunogen:
Recombinant antibody.
Host:
Rabbit
Clonality:
Monoclonal
Conjugate:
Unconjugated
Molecular Weight:
~ 70 kDa
Purity:
Protein A affinity purified
Product Form:
Recombinant Rabbit Monoclonal Antibody. 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
Target
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).
Tissue Specificity:
HSPA1B is testis-specific.
Sequence Similarities:
Belongs to the heat shock protein 70 family.
Post-Translational Modification:
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.
Cellular Location:
Cytoplasm. Cytoplasm > Cytoskeleton > Microtubule organizing center > Centrosome.
Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Database Links:
Entrez Gene: 3303?Human
Entrez Gene: 3304?Human
Entrez Gene: 15511?Mouse
Entrez Gene: 193740?Mouse
Entrez Gene: 24472?Rat
Entrez Gene: 294254?Rat
Omim: 140550?Human
Omim: 603012?Human
SwissProt: P08107?Human
SwissProt: P0DMV8?Human
SwissProt: P0DMV9?Human
SwissProt: P17879?Mouse
SwissProt: Q61696?Mouse
SwissProt: Q07439?Rat
Unigene: 274402?Human
Unigene: 719966?Human
Unigene: 728810?Human
Unigene: 1950?Rat
Unigene: 228225?Rat
Synonyms:
DnaK type molecular chaperone HSP70 1 Antibody
Epididymis secretory protein Li 103 Antibody
FLJ54303 Antibody
FLJ54370 Antibody
FLJ54392 Antibody
FLJ54408 Antibody
FLJ75127 Antibody
Heat shock 70 kDa protein 1 Antibody
Heat shock 70 kDa protein 1/2 Antibody
Heat shock 70 kDa protein 1A/1B Antibody
Heat shock 70kDa protein 1A Antibody
Heat shock 70kDa protein 1B Antibody
Heat shock induced protein Antibody
HEL S 103 Antibody
Hsp70 Antibody
HSP70 1 Antibody
HSP70 1/HSP70 2 Antibody
HSP70 1B Antibody
HSP70 2 Antibody
HSP70 iA Antibody
HSP70-1/HSP70-2 Antibody
HSP70-1A Antibody
HSP70.1 Antibody
HSP70.1/HSP70.2 Antibody
HSP70I Antibody
HSP71_HUMAN Antibody
HSP72 Antibody
HSPA1 Antibody
HSPA1A Antibody
HSPA1B Antibody
Information:
Target information shown above is from the UniProt Consortium.
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