Recombinant Pig HSP70.2 Protein, His-tagged

• Cat.No.: HSP70.2-2742P
• Product Overview: Recombinant Pig HSP70.2 Protein (Met1-Asp641) with N-His tag was expressed in E. coli.

Specification

• 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. 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. 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. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.
• Source: E. coli
• Species: Pig
• Tag: N-His
• Form: Freeze-dried powder
• Molecular Mass: Predicted Molecular Mass: 71.3 kDa
  Accurate Molecular Mass: 71 kDa
• Protein length: Met1-Asp641
• Purity: > 90%
• Applications: Positive Control; Immunogen; SDS-PAGE; WB.
• 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 centigrade 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: Avoid repeated freeze/thaw cycles. Store at 2-8 centigrade for one month. Aliquot and store at -80 centigrade for 12 months.
• Storage Buffer: 20mM Tris, 150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT, 0.01% SKL, 5% Trehalose and Proclin300.
• Reconstitution: Reconstitute in 20mM Tris, 150mM NaCl (pH8.0) to a concentration of 0.1-1.0 mg/mL. Do not vortex.

Gene Information

• Gene Name: HSP70.2 heat shock protein 70.2 [ Sus scrofa (pig) ]
• Official Symbol: HSP70.2
• Synonyms: HSP70.2; heat shock protein 70.2; HSPA1A; HSPA1B; heat shock 70 kDa protein 1B; heat shock 70 kDa protein 2; heat shock 70kDa protein 1A; heat shock 70kDa protein 1B
• Gene ID: 396648
• mRNA Refseq: NM_213766
• Protein Refseq: NP_998931
• UniProt ID: Q6S4N2