Hsc70 antibody

Catalog No. ABIN190358

This Rat Monoclonal antibody specifically detects Hsc70 in WB, IHC, IP and ICC. It exhibits reactivity toward Hamster.

Quick Overview for Hsc70 antibody (ABIN190358)

Target: Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

Reactivity: Hamster

Host: Rat

Clonality: Monoclonal

Conjugate: This Hsc70 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunoprecipitation (IP), Immunocytochemistry (ICC)

Clone: 1B5

Product Details anti-Hsc70 Antibody

Purpose: Anti-Hsc70 (Hsp73) Antibody Rat Monoclonal Antibody

Cross-Reactivity: Chicken, Cow, Dog, Guinea Pig, Hamster, Human, Monkey, Mouse, Pig, Rabbit, Rat, Sheep

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

Isotype: IgG2a

Application Details

Application Notes: Western Blot: 0.1 μg/mL
Immunoprecipitation: 5 μg/mL
Immunohistochemistry: 5 μg/mL
Immunocytochemistry: 5 μg/mL

Restrictions: For Research Use only

Handling

Format: Liquid

Reconstitution: Dilute in PBS or medium which is identical to that used in the assay system.

Concentration: Lot specific

Buffer: Phosphate buffered saline, pH 7.2, 0.1 mM PMSF in 50 % glycerol

Storage: 4 °C,-20 °C

Storage Comment: Store frozen product at or below -20°C. Thawed product may be stored for 2-4 weeks at 4°C. For optimal storage, aliquot and store at -20°C.

Target Details for Hsc70

Target: Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

Alternative Name: HSPA8 / HSC70

Background: Heat shock cognate 71 kDa protein,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}.,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.

Gene ID: 600816

UniProt: P11142