Recombinant Mouse Heat Shock 70 Kda Protein 1B (HSPA1B) Protein (His-SUMO)

Name: Recombinant Mouse Heat Shock 70 Kda Protein 1B (HSPA1B) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09522P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Heat Shock 70 Kda Protein 1B (HSPA1B) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P17879
Target Symbol	HSPA1B
Synonyms	Hspa1b; Hcp70.1; Hsp70-1; Hsp70a1; Hspa1; Heat shock 70 kDa protein 1B; Heat shock 70 kDa protein 1; HSP70.1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	AKNTAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDAVVQSDMKHWPFQVVNDGDKPKVQVNYKGESRSFFPEEISSMVLTKMKEIAEAYLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRGTLEPVEKALRDAKMDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTRDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAERYKAEDEVQRDRVAAKNALESYAFNMKSAVEDEGLKGKLSEADKKKVLDKCQEVISWLDSNTLADKEEFVHKREELERVCSPIISGLYQGAGAPGAGGFGAQAPPKGASGSGPTIEEVD
Expression Range	2-642aa
Protein Length	Full Length of Mature Protein
Mol. Weight	86.0kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target 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. 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.
Subcellular Location	Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families	Heat shock protein 70 family
Database References	KEGG: mmu:15511 STRING: 10090.ENSMUSP00000128525 UniGene: Mm.372314
Tissue Specificity	Testis-specific.

Gene Functions References

binding of IL-5 to IL-5Ralpha receptors enhances angiogenic responses by stimulating the expression of HSP70-1 via the eNOS signaling pathway. PMID: 28317868
The present study clearly demonstrated that the ectromelia virus infection upregulates the expression of Hspa1b in order to promote its replication. PMID: 29749430
HSP70 expression is up-regulated in fatty liver. PMID: 29631603
CM-695, a small molecule that induces the expression of the HSPA1A/B genes, increases the vessel wall levels of Hsp70 and prevents thrombosis at least as efficiently as rivaroxaban without increasing bleeding risk. PMID: 28837204
mHSP70407-426 could assist VEGF to display enhanced anti-tumor effects, which are important for the further application of mHSP70407-426 to enhance antigen-specific immune responses PMID: 29572180
Extracellular Hsp70 and Hsp90, either in soluble form or secreted as part of exosomes from tumor cells, are responsible for tumor induction of cachexia. PMID: 28928431
HSP70 functions as a negative regulator in the TGF-beta- stimulated VEGF synthesis in osteoblasts, and that the suppressive effect of HSP70 is exerted via regulation of p38 MAP kinase. PMID: 29179216
The data implicate an involvement of Hsp70 oxidatively damaged protein degradation by the 20S proteasome. PMID: 27498116
interaction between BAG3 and HSP70 is essential for BAG3 to stabilize small heat shock proteins and maintain cardiomyocyte protein homeostasis PMID: 28737513
Data show that Klotho protein is present in the heart, and reduced levels of myocardial Klotho in aging mice is accompanied by lower levels heat shock protein 70 (HSP70) in the myocardium. PMID: 28152512
analysis of the intracellular pathways implicated in Hsp70 regulated signal transduction showed the involvement of both PI3K/AKT and NF-kappaB. PMID: 27925208
HSPA1A/B induction is a novel approach to delay thrombus formation with minimal bleeding risk in knockout mice PMID: 26976620
Hsp70 expression was observed trophoblast cells and decidual cells and was relatively constant throughout the pregnancy. PMID: 26799792
The results of comparative analysis of interaction between the protein cytotoxic complex Tag 7-Hsp70 and the Tag 7 component of this complex with TNFR1 receptor in solution and in tumor cells are presented. PMID: 27021371
the protective effect of HSP70 may be associated with inhibition of NF-kappaB and stimulation of NOS/NO signaling pathways PMID: 26215736
activation of the HSP70-TLR4 axis, stimulated at least in part by albumin, in the tubular cell is a newly identified mechanism associated with induction of tubulointerstitial inflammation. PMID: 26398934
Knockdown lines were created for specific DSBs in regions of the chromosome that are coding for HSPA1B. Clonogenic cell survival was significantly lower in irradiated Hsp70 KD cells with low mHsp70 expression, than in ctrl cells. PMID: 26197988
Hsp70.1-deficient mice were more resistant to developing experimental autoimmune encephalomyelitis (EAE) compared with their wild-type littermates, suggesting Hsp70.1 plays a role in promoting myelin oligodendrocyte glycoprotein specific T cell response. PMID: 25153885
We report exosomal Hsp70 can expand and induce the activation of myeloid-derived suppressor cells PMID: 25603952
Results suggest that overexpression of Hsp70 may protect against brain ischemia via an anti-inflammatory mechanism by interrupting the phosphorylation of upstream of transcription factors. PMID: 25485480
These findings indicate that in mice HSP27 and HSP70 play a key role in the induction of cell-mediated immunity to carcinogenic polyaromatic hydrocarbons PMID: 25840912
Tumor-derived inducible heat-shock protein 70 (HSP70) is an essential component of anti-tumor immunity. PMID: 24662819
Hsp70 interacts with acidic glycopolymers that contain clustered sulfated and di-sialylated glycan moieties on a polyacrylamide backbone, but not with neutral or mono-sialylated glycopolymers. PMID: 24909693
HSP70 has a role in liver regeneration after partial hepatectomy in mice PMID: 24357103
It plays a protective role against AP-induced liver injury. PMID: 24219791
BAG-1 possesses an ubiquitin-like domain (Ub-LD) responsible for proteasomal association and for promoting substrate release from Hsc70/Hsp70 in vitro by accelerating the chaperone ATP/ADP exchange rate. PMID: 23178238
Functional study of Hsp70 revealed that decreased expression of Hsp70 diminished the apoptosis induced by Sialic acid-binding lectin. It is suggested that Hsp70 participates in the antitumor effect of Sialic acid-binding lectin. PMID: 24173532
Exercise preconditioning in mice can prevent oxidative stress and apoptotic cell death in the kidney resulting from ischemic injury even under Hsp70 deficiency PMID: 23780557
Loss of the inducible Hsp70 delays the inflammatory response to skeletal muscle injury and severely impairs muscle regeneration. PMID: 23626847
study reports that carbonylation of HSP70 by reactive oxygen species is associated with the pathogenesis of contact hypersensitivity, suggesting possibility of HSP70-targeting therapy in contact hypersensitivity PMID: 23679814
Hsp70 is crucially involved in the labile phase of development of behavioral sensitization induced by a single morphine exposure, probably functioning as a molecular chaperone. PMID: 22647551
Inner ear supporting cell secreted HSP70 protects hair cells from apoptotic cell death. PMID: 23863716
Hsp70 is required for IKK activation and STAT1/IRF-1 promoter binding amid iNOS gene transactivation. PMID: 23419754
We confirmed that Hsp70 and TLR4 coimmunoprecipitate in lung tissue and MLECs. Hsp70-mediated NF-kappaB activation appears to depend upon TLR4. In the absence of TLR4, Hsp70 loses its protective effects in endothelial cells. PMID: 23817427
Acetylation of hsp70 Regulates SUMOylation of Vps34 and Its Association with Beclin 1 in Breast Cancer Cells PMID: 23569248
Formation of HSP70- and MDM2-dependent protein coaggregates in tumours with high levels of these two proteins could be one of the mechanisms by which mutant p53 is stabilized. PMID: 23251530
Hsp70 induction is sufficient to prevent NRG1-induced demyelination by enhancing the proteasomal degradation of c-Jun. PMID: 23240583
This study provides evidence for an inhibitory effect of HSP70 on UV-induced wrinkle formation. PMID: 23096703
Collectively, these results support a novel axis of type I interferon-dependent antiviral immunity in the measles virus-infected brain that is driven by hsp70. PMID: 23135720
Opposing actions of heat shock protein 90 and 70 regulate nicotinamide adenine dinucleotide phosphate oxidase stability and reactive oxygen species production. PMID: 23023377
Higher sensitivity of ES cells to proteotoxic stress may be related with lower capacity of HSP70 expression. PMID: 22617454
cholesterol and more likely 7beta-OH may exert their pro-atherogenic effects by lowering hsp70 protein production and inhibiting glutathione synthesis by macrophages present in the arterial wall PMID: 22896903
effect of oxidative stress on the process of spermatogenesis in terms of hsp70 expression was studied. For creating different oxidative PMID: 22900316
Heat shock protein 70 (rSj648/hsp70) induces high protection against schistosome-infection contributing to predominant Th1 reaction and the correlation with high expression of IFN-gamma. PMID: 22590864
The data herein supports the theory that HSP70 is involved in normal skin protein configuration and the cellularity of early wound healing. PMID: 22275297
The Hsp70 inhibits H(2)O(2)-induced nucleolar fragmentation through the translocation of Hsp70 into nucleolar and its protection against impairment of nucleolin. PMID: 21960124
There was a significant induction of HSP70 in the arthritic chondrocytes treated with laser therapy. PMID: 21749827
Extracellular HSP70 acting via TLR2 and its obligate downstream adaptor molecule, MyD88, activate NFkappaB, causing cardiomyocyte inflammation and decreased contractility. PMID: 21817814
HSP70i was necessary and sufficient to accelerate depigmentation in vitiligo-prone Pmel-1 mice, accompanied by lasting phenotypic changes in dendritic cell subpopulations. PMID: 21978301
These results indicate that HSP70 alone is not sufficient to reduce MPTP-induced dopaminergic neuronal damage. PMID: 21782904

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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