Rabbit HSPA1A Polyclonal Antibody | anti-HSPA1A antibody

Anti HSPA1A polyclonal antibody

Cat. Num. AAA1560257

• Gene Names: HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A
• Reactivity: Human; Other species were not tested
• Applications: Western Blot, Immunohistochemistry
• Purity: Antigen affinity purification
• Synonyms: HSPA1A; Polyclonal Antibody; Anti HSPA1A polyclonal antibody; Heat shock 70 kDa protein 1A; HSP70-1; Heat shock 70 kDa protein 1; HSP72; HSPA1; HSX70; anti-HSPA1A antibody

• Host: Rabbit
• Reactivity: Human; Other species were not tested
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Antigen affinity purification
• Form/Format: Liquid. Supplied as solution form in PBS, pH7.4, containing 0.05% proclin300, 50% glycerol.
• Concentration: 0.5mg/ml (varies by lot)

• Applicable Applications for anti-HSPA1A antibody: Western Blot (WB), Immunohistochemistry (IHC)
• Application Notes: WB: 1:2000-1:8000; IHC: 1:200-1:400
• Immunogen: Recombinant protein of human HSPA1A (Met1-Asp641)
• Conjugation: Unconjugated
• Dry Ice Shipment: Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
• Preparation and Storage: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 4 degree C for frequentUse. Store at -20 to -80 degree C for twelve months from the date of receipt.

Western Blot (WB)

Related Product Information for anti-HSPA1A antibody

HSPA1A, collectively known as HSP70 (also referred to HSP72), is a stress-inducible member of heat-shock protein 70 (HSP70) proteins which are highly conserved chaperons implicated in protein folding, protein refolding, protein transport, and protein targeting. Encoded by two closely linked, intronless and stress-inducible genes, HSPA1A and HSPA1B differ by only two amino acids and are believed to be fully interchangeable proteins. HSPA1A is a cytosol/nuclear protein able to translocate between cytoplasm and nucleus. Generally, HSPA1A is thought to be expressed in unstressed normal cells at low or undetectable levels. Expression of HSPA1A protein can be highly activated by various stressful stimuli. Significant up-regulation of HSPA1A has been found in various tumors. Recently it has been reported that HSPA1A can be constitutively expressed in selected cell types. HSP70 is a useful marker for exosome. This antibody well recognized the endogenous HSP70 protein in multiple cell lines.(21373891)

Product Categories/Family for anti-HSPA1A antibody

Primary antibody

References

PubMed: 24012426; PubMed: 26865365; PubMed: 24318877

NCBI and Uniprot Product Information

• NCBI GI #: 194248072
• NCBI GeneID: 3303
• NCBI Accession #: NP_005336.3
• NCBI GenBank Nucleotide #: NM_005345.5
• UniProt Accession #: P0DMV8; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0; B4E3B6; P08107
• Molecular Weight: 70,052 Da
• NCBI Official Full Name: heat shock 70 kDa protein 1A/1B
• NCBI Official Synonym Full Names: heat shock 70kDa protein 1A
• NCBI Official Symbol: HSPA1A
• NCBI Official Synonym Symbols: HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A
• NCBI Protein Information: heat shock 70 kDa protein 1A/1B; HSP70-1/HSP70-2; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70 kDa protein 1/2; dnaK-type molecular chaperone HSP70-1
• UniProt Protein Name: Heat shock 70 kDa protein 1A
• Protein Family: Heat shock 70 kDa protein
• UniProt Gene Name: HSPA1A
• UniProt Synonym Gene Names: HSP721 PublicationManual assertion based on opinion iniRef.41; HSP70-12 PublicationsManual assertion based on opinion iniRef.4; HSP70.1

NCBI Description

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]

Uniprot 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).