Heat shock cognate 71 kDa protein (Hspa8), mouse, recombinant

Organism: Mus musculus (Mouse). Source: E.coli. Expression Region: 2-646aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: SKGPAVGIDL GTTYSCVGVF QHGKVEIIAN DQGNRTTPSY VAFTDTERLI GDAAKNQVAM NPTNTVFDAK RLIGRRFDDA VVQSDMKHWP FMVVNDAGRP KVQVEYKGET KSFYPEEVSS MVLTKMKEIA EAYLGKTVTN AVVTVPAYFN DSQRQATKDA GTIAGLNVLR IINEPTAAAI AYGLDKKVGA ERNVLIFDLG GGTFDVSILT IEDGIFEVKS TAGDTHLGGE DFDNRMVNHF IAEFKRKHKK DISENKRAVR RLRTACERAK RTLSSSTQAS IEIDSLYEGI DFYTSITRAR FEELNADLFR GTLDPVEKAL RDAKLDKSQI HDIVLVGGST RIPKIQKLLQ DFFNGKELNK SINPDEAVAY GAAVQAAILS GDKSENVQDL LLLDVTPLSL GIETAGGVMT VLIKRNTTIP TKQTQTFTTY SDNQPGVLIQ VYEGERAMTK DNNLLGKFEL TGIPPAPRGV PQIEVTFDID ANGILNVSAV DKSTGKENKI TITNDKGRLS KEDIERMVQE AEKYKAEDEK QRDKVSSKNS LESYAFNMKA TVEDEKLQGK INDEDKQKIL DKCNEIISWL DKNQTAEKEE FEHQQKELEK VCNPIITKLY QSAGGMPGGM PGGFPGGGAP PSGGASSGPT IEEVD. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: 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 of HSP70, 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 of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones 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. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21. Reference: "Critical role for Gimap5 in the survival of mouse hematopoietic stem and progenitor cells." Chen Y., Yu M., Dai X., Zogg M., Wen R., Weiler H., Wang D. J. Exp. Med. 208:923-935(2011). Function: nan