Recombinant Mouse Prohibitin (PHB) Protein (His)

Name: Recombinant Mouse Prohibitin (PHB) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03405P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Phb.

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Product Overview

Description	Recombinant Mouse Prohibitin (PHB) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P67778
Target Symbol	PHB
Synonyms	Phb; Prohibitin; B-cell receptor-associated protein 32; BAP 32
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	RFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIYTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHL
Expression Range	41-173aa
Protein Length	Partial
Mol. Weight	20.5 kDa
Research Area	Transcription
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	Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus. Plays a role in adipose tissue and glucose Homeostasis in a sex-specific manner. Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells.; In the mitochondria, together with PHB2, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan (Probable). The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner. Regulates mitochondrial respiration activity playing a role in cellular aging. The prohibitin complex plays a role of mitophagy receptor involved in targeting mitochondria for autophagic degradation. Involved in mitochondrial-mediated antiviral innate immunity, activates DDX58/RIG-I-mediated signal transduction and production of IFNB1 and proinflammatory cytokine IL6.; In the nucleus, acts as a transcription coregulator, enhances promoter binding by TP53, a transcription factor it activates, but reduces the promoter binding by E2F1, a transcription factor it represses. Interacts with STAT3 to affect IL17 secretion in T-helper Th17 cells.; In the plasma membrane, cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates. Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation.; (Microbial infection) In neuronal cells, cell surface-expressed PHB is involved in human enterovirus 71/EV-71 entry into neuronal cells specifically, while membrane-bound mitochondrial PHB associates with the virus replication complex and facilitates viral replication. May serve as a receptor for EV71.
Subcellular Location	Mitochondrion inner membrane. Nucleus. Cell membrane. Cytoplasm.
Protein Families	Prohibitin family
Database References	KEGG: mmu:18673 STRING: 10090.ENSMUSP00000119603 UniGene: Mm.263862
Tissue Specificity	Widely expressed in different tissues.

Gene Functions References

prohibitin is an important negotiator protein that regulates dopaminergic cell death in substantia nigra and their protection in ventral tegmental area in Parkinson's Disease. PMID: 28062948
Elevated PHB levels in EAE brains signify the role of PHB in regulating ROS and implies PHB's role in oxidative stress. PMID: 29242126
obesity-associated hyperinsulinemia promotes tumor development by facilitating dormant mutant to manifest and reveals a sex-dimorphic role of PHB in adipose-immune interaction or immunometabolism. PMID: 26751773
results demonstrate that the H19-Igf2 axis is negatively regulated by CTCF-PHB1 cooperation and that H19 is involved in modulating the growth-suppressive effect of PHB1 in the liver. PMID: 27687727
Study shows that PHB is highly expressed in white adipose tissue and liver which expression is regulated by estrogen. PMID: 26048717
This study identifies a novel signaling pathway composed of miR-361 and PHB1 that regulates mitochondrial fission program and apoptosis. PMID: 25501599
A role for PHB in GnRH-induced cell death in mature gonadotropes, which is crucial for the normal development and function of the reproductive axis. PMID: 24085822
Data indicate that phosphorylation of Tyr114 and Tyr259 of prohibitin (PHB) is critical for the association of PHB with FcRI and Syk. PMID: 24023254
Phb1/2 and the CD86 cytoplasmic domain cooperate to mediate CD86 signaling in a B cell through differential phosphorylation of distal signaling intermediates required to increase IgG1. PMID: 23241883
Findings suggest that PHB protects against colitis-associated cancer by modulating p53- and STAT3-mediated apoptosis. PMID: 22869582
Phb1 deficiency is a potential driver of chronic liver diseases by inducing hepatocyte damage and inflammation. PMID: 22951295
Identified PHB as an important protein in adipocyte differentiation. Furthermore, the overexpression of PHB in 3T3-L1 fibroblasts was sufficient to induce adipogenesis. PMID: 22124450
PHB1 and PHB2 are critical mediators in promoting 3T3-L1 adipocyte differentiation and may be the potential targets for obesity therapies PMID: 22479600
These results suggest that under inflammatory conditions there is decreased expression of vitamin D receptor resulting in decreased expression of prohibitin. Vitamin D deficiency decreased the expression of vitamin D receptor and prohibitin. PMID: 22537547
This study demonstrates that prohibitin (PHB) is an estrogen-regulated gene and that PHB is essential for mouse uterine development and adult function and selectively required for estrogen-regulated gene expression. PMID: 21209023
Prohibitin is involved in oxidative stress signaling in the retina and retinal pigment epithelium. PMID: 20832420
Includes the study of an upstream ORF in this gene, and shows that it functions to reduce protein levels by ~58%. PMID: 19372376
BRE has a role in the regulation of key proteins of the cellular stress-response machinery, including prohibitin and p53 PMID: 16518872
Results indicate that PHB functions as a transcriptional corepressor for ERalpha in vitro and in vivo, and that its heteromerization with REA acts as a novel mechanism to limit its corepressor activity. PMID: 17932104
Differential expression of prohibitin and regulation of apoptosis in wild-type and COX-2 null mouse embryonic fibroblasts. PMID: 19013772

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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.