Recombinant Human Prohibitin (PHB) Protein (His)

Name: Recombinant Human Prohibitin (PHB) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10084P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Prohibitin (PHB) 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	P35232
Target Symbol	PHB
Synonyms	Epididymis luminal protein 215; Epididymis secretory sperm binding protein Li 54e; HEL 215; HEL S 54e; PHB; PHB_HUMAN; PHB1; Prohibitin
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ
Expression Range	1-272aa
Protein Length	Full Length
Mol. Weight	33.8kDa
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.
Subcellular Location	Mitochondrion inner membrane. Nucleus. Cytoplasm. Cell membrane.
Protein Families	Prohibitin family
Database References	HGNC: 8912 OMIM: 176705 KEGG: hsa:5245 STRING: 9606.ENSP00000300408 UniGene: Hs.514303
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
Results show that PHB expression is significantly increased in metastatic prostate cancer and represents a strong marker predicting survival, along with ALDH6A1 and HSP27. PMID: 30396985
Data suggest that prohibitin (PHB) plays a crucial role in integrating cell signaling events with metabolic switches, and may serve as a potential target for cancer immunotherapeutic [Review]. PMID: 29222040
prohibitin 1 regulates tumor cell apoptosis via the interaction with X-linked inhibitor of apoptosis protein PMID: 27025967
Up regulation of PHB in relapsing vs remission MS patients imply the potential use of PHB to clinically evaluate subclinical disease status towards prognosis of an oncoming relapse PMID: 29242126
Study gives attention to the functional role and regulatory mechanism of PHB proteins in cardiovascular health and diseases (VCD) and its associated implications. Various molecular pathways involved in PHB function and its regulation are analyzed. In neoplasm, PHB is shown to act through many mechanisms by acting as oncogene, tumor suppressor, antioxidant, antiapoptotic, in angiogenesis, autophagy etc. [review] PMID: 27557820
This study support the role of miR-195 as anti-proliferative miRNA via targeting of PHB1 in melanoma cells PMID: 29126391
Data (including data from studies using knockout mice) suggest that cell surface-expressed PHB is involved in Enterovirus 71 entry into neuronal cells; mitochondrial membrane-bound PHB associates with virus replication complex and facilitates viral replication. PMID: 29324904
The G to A transition but not the C-to-T transition in the 3'-UTR of prohibitin was associated with an increased risk of gastric cancer in Chinese population. PMID: 28294412
Case Report: imbalance between ROS and antioxidants together with failure of signal transduction in the glomerular slit membrane caused by prohibitin 2 abnormality could have contributed to nephrotic syndrome. PMID: 27812762
Study elucidates an important role of PHBP1 in promoting esophageal squamous cell carcinoma partly via increasing PHB expression. PMID: 28404970
Endoplasmic reticulum resident chaperone GRP78, mitochondrial protein Prohibitin and heterogeneous nuclear ribonucleoprotein hnRNPC (C1/C2) have been shown to interact with viral RNA. Hence it is proposed that these are the principle candidates governing endoplasmic reticulum stress-induced apoptosis in JEV infection. PMID: 28102850
PHB1 down regulation suppresses liver cancer and bile duct cancer tumorigenesis. PMID: 27981602
PHB has an unexpected nuclear role in human embryonic stem cells that is required for self-renewal and that it acts with HIRA in chromatin organization to link epigenetic organization to a metabolic circuit. PMID: 27939217
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
PHB promotes AR activation in ER-positive breast cancer. PMID: 28272969
High PHB expression is associated with breast cancer. PMID: 27485113
Data shows that PHB protein was overexpressed in gallbladder cancer tissues and significantly associated with histological grade, tumor stage and perineural invasion. PMID: 27084680
The present review focus is on recent developments in prohibitin (PHB) research in relation to ovarian granulosa cells physiological functions. [review] PMID: 26496733
We propose a model whereby in analogy to previous findings (e.g., the RAS-RAF signalling pathway), PHB can act as a signalling scaffold protein to assist in KDELR-dependent Src activation PMID: 26064897
a majority of patients with IgG4-related disease have antibodies against prohibitin. PMID: 25932630
PHB phosphorylated at threonine 258 and MIG-7 may play complementary roles in the initiation and sustainment of the effects of growth factors and COX-2/PGE2 on cancer invasion/metastasis. PMID: 25575814
miR-27a was shown to be a significant tumor suppressor by targeting and decreasing PHB protein expression in glioma U251 cells. miR-27a targeting of PHB may be a novel potential therapeutic strategy for glioma PMID: 25777779
Less expression of prohibitin is associated with increased paired box 2 in renal interstitial fibrosis PMID: 22949832
A protective role of PHB that is dependent on pS727-Stat3 to prevent mitochondrial dysfunction in intestinal epithelial cells. PMID: 24975845
Knockdown of prohibitin expression promotes glucose metabolism in eutopic endometrial stromal cells from women with endometriosis. PMID: 25444511
we have provided a modified method for isolating and identifying membrane proteins and demonstrated that PHB1 may be a promising biomarker for early diagnosis and therapy of pancreatic (and potentially other) cancers. PMID: 25344214
PHB lies downstream of ERalpha and mediates estrogen-dependent Paclitaxel resistance signaling cascades PMID: 24376711
The study suggest that the tumor suppressing action of prohibitin is probably associated with luteinizing hormone mediated protection role against ovarian epithelial carcinoma. PMID: 24966933
The T allele of the rs6917 polymorphism was associated with reduced PHB mRNA levels. PMID: 24879411
Findings provide new insights into the function of prohibitin in transcriptional regulation and uncover a BASP1-prohibitin complex that plays an essential role in the PIP2-dependent recruitment of chromatin remodeling activities to the promoter. PMID: 24166496
Vi released by Salmonella typhi interacts with the membrane prohibitin complex and inhibits IL-2 secretion from T cells stimulated through the T-cell receptor (TCR). PMID: 24470505
PHB expression was crucial for maintenance of oncogenic ERK-driven pancreatic tumorigenesis PMID: 24568222
Results of the present study confirmed that the expression and distribution of PHB, which is a nuclear matrix protein, affect the apoptosis of HaCaT cells PMID: 24402549
Amplification at 17q21.33 is a recurrent feature of breast cancer that forms part of a 'firestorm' pattern of genomic aberration. PHB is not a driver of amplification, however PHB may contribute to high grade breast cancer. PMID: 24247619
Persistent PAR1 signaling due to the absence of membrane PHB and decreased PAR1 degradation caused by the upregulation of intracellular PHB in cancer cells may render them highly invasive. PMID: 24732013
The different subcellular localization of PHB1 in non-small cell lung cancer cells and the loss of the membrane-associated PHB1 probably related to the tumorigenesis and progression of NSCLC. PHB1 may play different roles in various types of NSCLC. PMID: 24133587
Prohibitin is regulated by miR-26a and promotes glioma progression and angiogenesis. PMID: 23870455
Prohibitin may be associated with breast cancer. PMID: 23715748
Studies indicate that in response to stimulation with antigen, PHB1 translocated to plasma membrane lipid rafts to form a ternary complex with the high-affinity IgE receptor FcepsilonRIgamma and the nonreceptor tyrosine kinase Syk. PMID: 24023253
prohibitin and prohibiton (PHB2) contribute to PIG3-mediated apoptosis by binding to the PIG3 promoter (TGYCC)15 motif PMID: 24388982
These results suggest that the altered localization and expression of PHB, as well as its co-localization with related oncogenes and tumor suppressor genes, can affect the apoptosis of Mz-ChA-1 cells. PMID: 24380853
Our data suggest that miR-27 is an anti-adipogenic microRNA partly by targeting prohibitin and impairing mitochondrial function. PMID: 24133204
Decreased expression of prohibitin protein is closely associated with poor prognosis and metastasis in nasopharyngeal carcinoma. PMID: 22728421
PHBs are localized on the human platelet membrane and are involved in PAR1-mediated platelet aggregation. PMID: 22212092
Here, we review the signal transduction pathways of PHB and its role in the pathogenesis of diseases. PMID: 23327602
Calreticulin and prohibitin were identified to be novel candidate biomarkers for adrenocortical carcinomas. PMID: 23587357
Six investigations were identified for the analysis of association between the prohibitin 3' untranslated region C > T gene polymorphism and cancer risk. PMID: 22994754
Missense mutation in prohibitin may be associated with breast tumor development and/or progression. PMID: 23244120
In schizophrenia, there were significantly more prohibitin-expressing oligodendrocytes in the right dorsolateral white matter area, suggesting involvement in mitochondrial and/or cell-cycle dysfunction. PMID: 22711522

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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.

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