Anti-HSC 70 antibody

Rs. 50,211.00
SKU stj93597

General Information

Product name Anti-HSC 70 antibody
Short Description
Description Rabbit polyclonal to HSC 70.
Applications WB,ELISA
Dilution range WB 1:500-1:2000ELISA 1:20000
Protein Name Anti-HSC 70 antibody
Immunogen Synthesized peptide derived from human HSC 70.
Storage Instruction Store at -20°C, and avoid repeat freeze-thaw cycles.
Type of Usage For Research Use Only (RUO).

Product Properties

Host Rabbit
Clonality Polyclonal
Reactivity Mouse,Rat
Conjugation Unconjugated
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Target

Gene ID
Gene Symbol
Molecular Weight 72 kDa
Database Links
Alternative Names Heat shock cognate 71 kDa protein antibody
Heat shock 70 kDa protein 8 antibody
Lipopolysaccharide-associated protein 1 antibody
LAP-1 antibody
LPS-associated protein 1 antibody
HSC70 antibody
HSP73 antibody
HSPA10 antibody
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 of HSP70, 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 of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones 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 . Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes . Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 .
Cellular Localization Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
Tissue Specificity Ubiquitous.
Swiss-Prot Key

 

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