Recombinant Human 10 Kda Heat Shock Protein, Mitochondrial (HSPE1) Protein (His)

Name: Recombinant Human 10 Kda Heat Shock Protein, Mitochondrial (HSPE1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08324P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human 10 Kda Heat Shock Protein, Mitochondrial (HSPE1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P61604
Target Symbol	HSPE1
Synonyms	10 kDa chaperonin; 10 kDa heat shock protein mitochondrial; 10 kDa heat shock protein; mitochondrial; CH10_HUMAN; Chaperonin 10; Chaperonin 10 homolog; CPN10; cpn10 homolog; Early pregnancy factor; Early-pregnancy factor; EPF; GROES; GroES homolog; Heat shock 10kD protein 1 chaperonin 10; Heat shock 10kDa protein 1; Heat shock 10kDa protein 1 chaperonin 10; Heat shock protein family E (Hsp10) member; Heat-shock 10-kD protein; Hsp10; Hspe1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD
Expression Range	2-102aa
Protein Length	Full Length of Mature Protein
Mol. Weight	14.8kDa
Research Area	Neuroscience
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	Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
Subcellular Location	Mitochondrion matrix.
Protein Families	GroES chaperonin family
Database References	HGNC: 5269 OMIM: 600141 KEGG: hsa:3336 STRING: 9606.ENSP00000233893 UniGene: PMID: 29028811 miR-146a, miR-146b, and miR-155 are exerting anti-inflammatory properties by down-regulating IL-6 and IL-8, and influencing the expression of HSP10 in the activated endothelium PMID: 28662100 High expression of HSP10 is negatively associated with estrogen receptor/progesterone receptor status and might be a novel independent biomarker for poor prognosis in invasive ductal breast carcinoma. PMID: 27993580 EPF induces the differentiation of regulatory T cells and increases their immunosuppressive activities. PMID: 27840373 Cpn10 has a role in the spatial regulation of NPAT signaling PMID: 26429916 Hsp10 has a role in nuclear localization and lung cells response to cigarette smoke PMID: 25355063 Data show that that in presence of 300 mg/mL Ficoll the thermodynamic stability of each cpn10 monomer increases by over 30%, whereas the interfaces are stabilized by less than 10%. PMID: 21375247 HSP10 protein was detected only in oocytes from human preantral follicles, whereas in antral follicles, it was localised in oocytes, granulosa cells, theca cells and stroma cells. PMID: 19903031 Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. PMID: 11898127 The low stability of the monomeric unit suggests that folding and assembly reactions for cpn10 are coupled. PMID: 12220543 Cpn10 and placental lactogen are capable of stimulating the synthesis of type I collagen by human osteoblasts in culture PMID: 12703979 Identification of amino acids important for the assembly of the cpn10 heptamer. PMID: 14525625 complex mechanisms are involved in the protection by hsp10 against simulated ischemia and reoxygenation-induced myocyte death PMID: 15059967 The HSP10 plays a role in bone marrow cell differentiation other than being a mitochondrial co-chaperonin. PMID: 15590416 Chaperonin 10 and calgranulin A are identified as markers for diagnosis and screening of endometrial carcinoma. PMID: 15816004 the cpn10 interfaces can adapt to structural alterations without loss of either subunit-subunit affinity or heptamer specificity PMID: 15978542 biophysical analysis of dissociation equilibrium for the heptameric co-chaperonin proteins 10 from Aquifex aeolicus and human mitochondria PMID: 16100270 proteomic analysis of possible role of heat shock protein 10 in colorectal cancer PMID: 16502466 Results describe the time-resolved folding and assembly mechanism of the heptameric co-chaperonin protein 10 (cpn10) in vitro. PMID: 16979655 Investigation of single-nucleotide variations in the Hsp10 gene and their disease-causing potential. PMID: 17072495 In this review, we revise the involvement of Hsp10 in signal transduction pathways and its possible role in cancer etiology. PMID: 17278877 Data show that Hhsp10 formed fibrils from only the acidic unfolded state and Core peptide regions of these protein fibrils were determined by proteolysis followed by a combination of Edman degradation and mass spectroscopy analyses. PMID: 18329043 The effects of cpn 10 on cells of the oligodendrocyte lineage, were assessed. PMID: 18465204 In patients with serous ovarian carcinomas, gene expression analysis coupled with immunohistochemistry allowed the identification of HSP10 as an independent factor of progression-free survival. PMID: 18500265 Results describe a novel function of chaperonin 10 as a general differentiation factor, not limited to erythroid cells, and show how this biological effect is mediated by GSK-3alpha/beta. PMID: 19142874 HSP10 was identified as a new autoantigen in both autoimmune pancreatitis and fulminant type 1 diabetes. PMID: 19520060

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.