Recombinant Human Gankyrin Protein

Name: Recombinant Human Gankyrin Protein
Brand: Beta LifeScience
SKU: BL-2042NP
Availability: InStock

BL-2042NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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

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Product Overview

Description	Recombinant Human Gankyrin is produced by our E.coli expression system and the target gene encoding Met1-Gly226 is expressed.
Accession	O75832
Synonym	26S Proteasome Non-ATPase Regulatory Subunit 10; 26S Proteasome Regulatory Subunit p28; Gankyrin; p28(GANK); PSMD10
Gene Background	Gankyrin is a multicatalytic proteinase oncoprotein consists of 7 ankyrin repeats. Gankyrin overexpressed in most hepatocellular carcinomas. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4 to enhance the ubiquitinylation of p53 by MDM2. Gankyrin is also involved in progression of esophageal squamous cell carcinoma. Gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis.
Molecular Mass	24.43 KDa
Apmol Mass	26 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of PBS, 10% Glycerol, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.; Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.
Subcellular Location	Cytoplasm. Nucleus.
Database References	HGNC: 9555 OMIM: 300880 KEGG: hsa:5716 STRING: 9606.ENSP00000217958 UniGene: PMID: 30420909 the pro-malignant effects of Gankyrin in CRC cells PMID: 29883699 Low Gankyrin expression is associated with drug resistance in Breast Cancer. PMID: 29286612 the results demonstrated that the lentivirus-mediated shRNA vector-based RNAi expression system is an efficient method to silence PSMD10 gene expression in the MM RPMI-8226 cell line. It may provide a basis to study the role of PSMD10 in tumor cells, and may be a reliable gene therapy strategy in the clinic PMID: 28677774 Gankyrin sustains PI3K/GSK-3beta/beta-catenin signal activation and promotes an aggressive colorectal cancer phenotype and disease progression. PMID: 27835604 PSMD10/gankyrin has a role in inducing autophagy to promote tumor progression through cytoplasmic interaction with ATG7 and nuclear transactivation of ATG7 expression PMID: 25905985 we conclude that FXR-Gank-TSPs-Stem cells pathway is a key determinant of liver cancer in animal models and in pediatric liver cancer. Our data provide a strong basis for development of FXR-Gank-based therapy for treatment of patients with hepatoblastoma PMID: 28535186 p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for regulatory particle engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly. PMID: 28689658 gankyrin regulates HIF-1alpha protein stability and cyclin D1 expression, ultimately mediating FSH-driven ovarian cancer cell proliferation PMID: 26364616 The positive feedback regulation involving gankyrin and Nrf2 modulates a series of antioxidant enzymes, thereby lowering intracellular ROS and conferring a steadier intracellular environment, which prevents mitochondrial damage and cell death induced by excessive oxidative stress. PMID: 27091842 Gankyrin enhanced gastric cancer cell proliferation by regulating cell cycle-related proteins and by activating PI3K/AKT signaling pathway. Gankyrin played an important role in gastric carcinogenesis and could be a potential effective therapeutic target for enhancing chemosensitivity to 5-fluorouracil and cisplatin. PMID: 28653901 gankyrin is an oncoprotein that can be modified by small molecules in tumor cell lines PMID: 27046077 Gankyrin overexpression activates mTORC1 signaling and accelerating TSC2 degradation in colorectal tumor cells. PMID: 26975632 Gankyrin is an oncoprotein that facilitates the degradation of two key tumor suppressors, namely, Rb and p53. Gankyrin is involved in the regulation of cell signaling pathways, with particular reference to RhoA/ROCK/PTEN/PI3K/Akt, beta-catenin, IL-6/STAT3, and IL-1beta/IRAK-1 inflammatory signaling. Review. PMID: 26819208 Gankyrin-overexpressed non-small cell lung cancer patients had a significantly shorter survival time PMID: 26554593 Results identified rs111638916 SNP in the PSMD10 3'-UTR as a risk factor for gastric cancer (GC) and acted as a tumor promoting factor. SNP rs111638916 was also regulated by miR-505, resulting in its up-regulation in patients with GA and AA genotypes. PMID: 26394032 p28GANK expression was increased in metastatic ESCC tissues and cells, and p28GANK knockdown decreased the metastatic ability of ESCC cells. PMID: 25634618 This study identifies gankyrin, for the first time, as new potential predictive and oncogenic factor of well-differentiated/dedifferentiated liposarcoma, suggesting the potential for service as a future Liposarcoma therapeutic approach. PMID: 25238053 On the base results of present study one can suggests the p28GANK being useful as a predictive marker for patient prognosis and a novel therapeutic target for gastric cancer. PMID: 25842830 IL-1beta stimulation causes sequential phosphorylation of IRAK-1, c-Jun N-terminal kinase, and p300 and enhances recruitment of the p300/CBP/NF-Y complex to Gankyrin promoter PMID: 25294684 Gankyrin is aberrantly expressed beginning at the initiation stage and plays an important role in the initiation, promotion, and progression of hepatocarcinogenesis. PMID: 24999092 Gankyrin may be functional in cervical carcinogenesis and metastasis. PMID: 24751719 MiR-605 directly targets and represses PSMD10 expression. PMID: 25131931 The intensity of gankyrin expression was 'positive' in two cases (20%) and 'strongly positive' in eight cases (80%). PMID: 24460153 Gankyrin deletion abrogated the increased metastatic potential of breast cancer cells under hypoxic conditions partly through regulating Ecadherin. PMID: 24337075 Gankyrin is crucial for cholangiocarcinoma carcinogenesis and metastasis by activating IL-6/STAT3 signaling pathway through down-regulating Rb protein. PMID: 24037855 Activation of the interleukin (IL)-8 signaling pathway by Gankyrin. PMID: 23576566 Data indicate that miR-214 down-regulated the expression of PSMD10 (gankyrin) and ASF1B, and gankyrin inhibition induced an increase of P53 mRNA levels. PMID: 23100276 In colorectal cancer development, gankyrin would control stem cell behavior by regulating the expression of stemness factors. PMID: 23508981 findings suggest that Gankyrin is crucial for breast cancer metastasis PMID: 22890318 gankyrin was identified in normal breasts and overexpressed in invasive breast cancers. The overexpression of gankyrin was associated with extensive intraductal carcinoma and ErbB2 expression in breast cancer. PMID: 23276718 Increased expression of p28GANK is correlated with glioma. PMID: 22913315 the roles and underlying mechanisms by which gankyrin is involved in tumorigenesis and cancer metastasis PMID: 22913272 Knockdown of HURP inhibits the proliferation of hepacellular carcinoma cells via downregulation of gankyrin and accumulation of p53. PMID: 22230478 Upregulation of p28(GANK) expression subsequently enhanced the transcription activity of beta-catenin. PMID: 21691299 Gankyrin overexpression is a prevalent event in human oral cancer and occurs during the early stages of oral carcinogenesis, thus being a viable therapeutic or chemopreventive target in oral cancer PMID: 21868508 we detected a significant correlation between p28(GANK) expression and p-AKT levels in a cohort of hepatocellular carcinoma biopsies, and the combination of these two parameters is a more powerful predictor of poor prognosis. PMID: 21254169 these findings suggest that down-regulation of P28GANK gene expression could sensitize osteosarcoma cells to chemotherapeutic drugs by down-regulation of the MDR-1 and Bcl-2 and up-regulation of Bax gene expression. PMID: 21287809 Gankyrin could enhance pancreatic cancer cell proliferation by promoting cell cycle progression and p53 degradation. PMID: 20483533 analysis of how gankyrin unfolds under force via multiple distinct pathways PMID: 20371329 Gankyrin is a key regulator of Ras-mediated activation of Akt through inhibition of the downstream RhoA/ROCK pathway and thus plays an essential role in Ras-induced tumorigenesis. PMID: 20628200 Gankyrin was overexpressed in colorectal cancer tissues and cell lines compared to controls, and gankyrin expression was correlated with TNM stages and metastasis of CRC. PMID: 19901563 p28(GANK) has potential implications for hepatocellular carcinoma progression under the endoplasmic reticulum stress conditions PMID: 19736567 Overexpression of p28/gankyrin in HCC plays an important role and contributes to the metastasis potential in the process of carcinogenesis. PMID: 12174370 MAGE-A4 binds to gankyrin and suppresses its oncogenic activity. PMID: 12525503 gankyrin interactions with partner proteins are mediated by residues situated on its concave surface PMID: 14573599 X-ray structure of gankyrin. PMID: 14997555 The hepatocytic staining for p28(GANK) is clearly useful in differentiating hepatocyte-originated carcinoma from non-HCC. p28(GANK) may be used as an ancillary marker for the diagnosis of HCC. PMID: 15221469 Structural comparison with p16(INK4A) identified several residues of gankyrin that are potentially important for CDK4 binding PMID: 15379554 role of p28GANK as a highly expressed oncoprotein in hepatocellular carcinoma by in situ examination PMID: 15910504

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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.

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Recombinant Human Gankyrin Protein

Recombinant Human Gankyrin Protein

Product Overview

Target Details

FAQs