Anti-HSPA1A Rabbit pAb

Antibody type:Primary antibody

Label:Unconjugated

Modification:Unmodification

Isotype:Rabbit IgG

Host:Rabbit

Application:WB

Purify method:Affinity purified

Species:Human,Mouse,Rat

Gene Name:HSPA1A

Synonyms:HSP72; HSPA1; HSP70I; HSP70-1; HSP70.1; HSP70-1A; HEL-S-103

Gene Synonyms:

Gene Full Name:heat shock protein family A (Hsp70) member 1A

Gene Infomation: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]

Antigen:A synthetic peptide corresponding to a sequence within amino acids 500-600 of human HSPA1A (NP_005336.3).

Antigen Synonyms:Heat shock 70 kDa protein 1A

Clonality:Polyclonal antibody

Source:Human

Reaction:

Form:Liquid

Tested Applications:

• Western blot (1:100 to 1:500)
• Immunofluorescence (1:50 to 1:400)
• Immunohistochemistry (1:200 to 1:500)
• Flow cytometry analysis (1:200 to 1:500)
• Enzyme-linked Immunosorbent Assay (1:100-1:5000)

Note: Users are strongly advised to determine the optimal dilution of antibody to use for their specific applications.

Clone:

Dilution:WB1:1000 -1:3000(Optimal dilutions should be determined by the end user)

Mole Mass:70kDa

Location:Cytoplasm, Cytoskeleton, Nucleus

Concentration:

Sequence Similarity:

Gene Id:

SwissProt ID:P0DMV8

Unigene:3303

Nucleotide Accession:

Tissue specificity:

Storage:Store at -20°C. Avoid freeze / thaw cycles.

Buffer condition:PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Background:

Molar 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. 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).

Western Blot: 

Stability: The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.

Storage: Store at 4°C for frequent use. Stored at -20°C in a manual defrost freezer for one year without detectable loss of activity. Avoid repeated freeze-thaw cycles.

Notes: For In vitro laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.