HSP70 1A antibody (C-Term)

Catalog No. ABIN6262398

The Rabbit Polyclonal anti-HSP70 1A antibody has been validated for WB, IHC, ELISA, IF and ICC. It is suitable to detect HSP70 1A in samples from Human, Mouse and Rat. There are 2+ publications available.

Quick Overview for HSP70 1A antibody (C-Term) (ABIN6262398)

Target: HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))

Reactivity: Human, Mouse, Rat

Host: Rabbit

Clonality: Polyclonal

Conjugate: This HSP70 1A antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)

Product Details anti-HSP70 1A Antibody

Binding Specificity: C-Term

Specificity: HSP70 Antibody detects endogenous levels of total HSP70.

Predicted Reactivity: Pig,Bovine,Sheep,Xenopus

Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink^TM Coupling Resin (Thermo Fisher Scientific).

Immunogen: A synthesized peptide derived from human HSP70, corresponding to a region within C-terminal amino acids.

Isotype: IgG

Application Details

Application Notes: WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: Rabbit IgG in phosphate buffered saline , pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.

Preservative: Sodium azide

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

Storage: -20 °C

Storage Comment: Store at -20 °C. Stable for 12 months from date of receipt.

Expiry Date: 12 months

References for anti-HSP70 1A antibody (ABIN6262398)

Xian, Gong, Li, Guo, Jiang: "Exosomes with Highly Angiogenic Potential for Possible Use in Pulp Regeneration." in: Journal of endodontics, Vol. 44, Issue 5, pp. 751-758, (2018) (PubMed).

Shan, Wang, Xu, Wang, Cao, Liu, Zhu: "Aging as a Precipitating Factor in Chronic Restraint Stress-Induced Tau Aggregation Pathology, and the Protective Effects of Rosmarinic Acid." in: Journal of Alzheimer's disease : JAD, Vol. 49, Issue 3, pp. 829-44, (2016) (PubMed).

Target Details for HSP70 1A

Target: HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))

Alternative Name: HSPA1A

Background:

Description: 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). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).

Gene: HSPA1A

Molecular Weight: 70 kDa

Gene ID: 3303, 3304

UniProt: P0DMV8

Pathways: Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process