Anti-Hsc70 (Hsp73) Antibody

$367.00

Host	Quantity	Applications	Species Reactivity	Data Sheet
Rat	50ug	WB,IP,IHC,ICC	Human, Mouse, Rat, Rabbit, Guinea Pig, Hamster, Monkey, Sheep, Chicken, Bovine, Canine, Porcine

SKU: 11042-50 Categories: Antibody Products, Heat Shock and Stress Protein Antibodies, Products

Overview

Product Name Anti-Hsc70 (Hsp73) Antibody (11042-50)

Description Anti-Hsc70 (Hsp73) Antibody Rat Monoclonal Antibody

Target Hsc70 (Hsp73)

Species Reactivity Human, Mouse, Rat, Rabbit, Guinea Pig, Hamster, Monkey, Sheep, Chicken, Bovine, Canine, Porcine

Applications WB,IP,IHC,ICC

Host Rat

Clonality Monoclonal

Clone ID 1B5

Isotype IgG2a

Immunogen Hsc70 purified from sodium arsenite treated heat-resistant variants of Chinese hamster cells.

Properties

Form Liquid

Concentration Lot Specific

Formulation Phosphate buffered saline, pH 7.2, 0.1mM PMSF in 50% glycerol.

Buffer Formulation Phosphate Buffered Saline

Buffer pH pH 7.2

Buffer Cryopreservative 50% Glycerol

Format Purified

Purification Purified by Protein A affinity chromatography

Target Name Heat shock cognate 71 kDa protein

Target ID Hsc70 (Hsp73)

Uniprot ID P11142

Gene Name HSPA8

Gene ID 600816

Sequence Location Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.

Biological 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 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). 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 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). 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 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). 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 (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). Interacts with VGF-derived peptide TLQP-21 (PubMed:28934328). {PubMed:10722728, PubMed:11276205, PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:23990462, PubMed:24318877, PubMed:24732912, PubMed:27474739, PubMed:27916661, PubMed:28934328, PubMed:24121476, PubMed:26865365}.

Research Areas Heat Shock& Stress Proteins

Handling

Storage Store at 2 - 8°C. Do not Freeze.

Dilution Instructions Dilute in PBS or medium which is identical to that used in the assay system.

Application Instructions Western Blot: 0.1 ug/ml

Immunoprecipitation: 5 ug/ml

Immunohistochemistry: 5 ug/ml

Immunocytochemistry: 5 ug/ml

Data Sheet