HSPA1B antibody (AA 418-641) (HRP)

Catalog No. ABIN7154874

Product Details anti-HSPA1B Antibody (HRP)

Target: HSPA1B (Heat Shock 70kDa Protein 1B (HSPA1B))

Binding Specificity: AA 418-641

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This HSPA1B antibody is conjugated to HRP

Application: ELISA

Cross-Reactivity: Human

Purification: >95%, Protein G purified

Immunogen: Recombinant Human Heat shock 70 kDa protein 1B protein (418-641AA)

Isotype: IgG

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Preservative: 0.03 % Proclin 300
Constituents: 50 % Glycerol, 0.01M PBS, pH 7.4

Preservative: ProClin

Precaution of Use: This product contains ProClin: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C,-80 °C

Storage Comment: Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Target Details for HSPA1B

Target: HSPA1B (Heat Shock 70kDa Protein 1B (HSPA1B))

Alternative Name: HSPA1B (HSPA1B Products)

Synonyms: HSP70-1B antibody, HSP70-2 antibody, APG-2 antibody, HS24/P52 antibody, HSPH2 antibody, RY antibody, hsp70 antibody, hsp70RY antibody, ARABIDOPSIS THALIANA HEAT SHOCK COGNATE PROTEIN 70-1 antibody, AT-HSC70-1 antibody, HEAT SHOCK COGNATE PROTEIN 70 antibody, HEAT SHOCK PROTEIN 70-1 antibody, HSC70 antibody, HSP70-1 antibody, T22P11.90 antibody, T22P11_90 antibody, heat shock cognate protein 70-1 antibody, Hsp70 antibody, Hsp70-1 antibody, Hsp70.1 antibody, hsp68 antibody, HSPA1A antibody, HSPA1B antibody, HSPA2 antibody, HSP70.2 antibody, Hsp70-2 antibody, Hsp72 antibody, Hspa1 antibody, Hspa1a antibody, Hspa2 antibody, heat shock protein family A (Hsp70) member 1B antibody, heat shock protein family A (Hsp70) member 4 antibody, heat shock cognate protein 70-1 antibody, heat shock protein 1B antibody, heat shock protein 70.2 antibody, heat shock 70kDa protein 1A antibody, heat shock 70kD protein 1B (mapped) antibody, HSPA1B antibody, HSPA4 antibody, HSC70-1 antibody, Hspa1b antibody, HSP70.2 antibody, HSPA1A antibody

Background:

Background: 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).

Aliases: HSPA1B antibody, HSP72 antibody, Heat shock 70 kDa protein 1B antibody, Heat shock 70 kDa protein 2 antibody, HSP70-2 antibody, HSP70.2 antibody

UniProt: P0DMV9