Recombinant Human S-Phase Kinase-Associated Protein 2 (SKP2) Protein (His-SUMO)

Name: Recombinant Human S-Phase Kinase-Associated Protein 2 (SKP2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04545P
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 S-Phase Kinase-Associated Protein 2 (SKP2) 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	Q13309
Target Symbol	SKP2
Synonyms	CDK2/Cyclin A associated protein p45; Cyclin A/CDK2 associated protein p45; Cyclin-A/CDK2-associated protein p45; F box protein Skp2; F box/LRR repeat protein 1; F-box protein Skp2; F-box/LRR-repeat protein 1; FBL 1; FBL1; FBXL 1; FBXL1; FLB 1; FLB1; MGC1366; p45; p45skp2; S phase kinase associated protein 2 (p45); S phase kinase associated protein 2; S-phase kinase-associated protein 2; S-phase kinase-associated protein 2 E3 ubiquitin protein ligase; SKP 2; Skp2; SKP2_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQELLSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLAEHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRKNLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL
Expression Range	1-424aa
Protein Length	Full Length
Mol. Weight	63.8kDa
Research Area	Cancer
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	Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, YTHDF2, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-dependent manner, thereby regulating cell migration.; Through the ubiquitin-mediated proteasomal degradation of hepatitis C virus non-structural protein 5A, has an antiviral activity towards that virus.
Subcellular Location	Cytoplasm. Nucleus.
Database References	HGNC: 10901 OMIM: 601436 KEGG: hsa:6502 STRING: 9606.ENSP00000274255 UniGene: PMID: 29377618 Report that YAP is subject to non-proteolytic, K63-linked polyubiquitination by the SCF(SKP2) E3 ligase complex (SKP2), which is reversed by the deubiquitinase OTUD1. The non-proteolytic ubiquitination of YAP enhances its interaction with its nuclear binding partner TEAD, thereby inducing YAP's nuclear localization, transcriptional activity, and growth-promoting function. PMID: 29891922 BTrCP-FBXW2-SKP2 axis forms an oncogene-tumour suppressor-oncogene cascade to control cancer cell growth with FBXW2 acting as a tumour suppressor by promoting SKP2 degradation. PMID: 28090088 Result demonstrated that the overexpression of S-phase kinase-associated protein 2 (Skp2) was closely involved in the resistance of osteosarcoma cells to methotrexate and in the acquirement of EMT properties. PMID: 29620168 The role of USP18 in breast cancer provides a novel insight into the clinical application of the USP18/AKT/Skp2 pathway. PMID: 29749454 SKP2 promotes HCC progression and its nuclear functions of autophagy induction with CARM1 and AMPK, which may provide a potential target for HCC therapy. PMID: 29991055 The results of the present study revealed that miR340 serves a tumor suppressor role by influencing the proliferation, apoptosis, migration and invasion of HCC cell lines, which may be explained by the downregulation of SKP2 by miR340. PMID: 28944918 Our findings revealed that targeting Skp2 could be a promising therapeutic strategy for the treatment of Osteosarcoma PMID: 28627672 Levels of p21 and p27 were decreased in TACO or pAKT overexpressing HCC due to SKP2 upregulation. PMID: 27779207 Skp2 exhibited an oncogenic function in osteosarcoma cells. PMID: 28771075 The results suggest that Skp2 repression is important for sustaining tetraploid G1 arrest after cytokinesis blockade and is required to prevent uncoupled DNA replication and nuclear division without cytokinesis. PMID: 28648144 DCUN1D3 has a role in activating SCFSKP2 ubiquitin E3 ligase activity through cullin-1 neddylation and cell cycle progression in tumor cells with UV damage PMID: 27542266 The expression of p-Skp2 was associated with p-mTOR in GC cell lines and tissues. Interestingly, the combination of p-Skp2 and p-mTOR was a better predictor of survival than either factor alone PMID: 28446188 Atorvastatin strengthens Skp2 binding to FOXO1 or ICAM1, leading to ubiquitination and degradation. Skp2-dependent ubiquitination of major pathogenic molecules is the key mechanism for statin's protective effect on endothelial function in diabetes. PMID: 28802579 we identified that rottlerin exhibited its anti-tumor potential partly through inactivation of Skp2 in breast cancer PMID: 27582552 These findings indicated that SKP2 inhibition sensitized the prolactinoma cells to bromocriptine and helped promote apoptosis. PMID: 27488872 Skp2 suppressed p53 and inhibited PIG3-induced apoptosis, while Skp2B attenuated the function of PIG3 by inhibiting PHB. PMID: 27111245 Data suggest that targeting S-phase kinase associated protein 2 (SKP2) may serve as a potential radiosensitizer for developing effective therapeutic strategies against cervical cancer. PMID: 27317767 Data indicate a positive correlation of Skp2 and MTH1 expression in melanoma cell lines and patient specimens. PMID: 28947420 These results indicated that at least some oncogenic functions of BAG3 were mediated through posttranscriptional regulation of Skp2 via antagonizing suppressive action of miR-21-5p in ovarian cancer cells. PMID: 28624440 High SKP2 expression is associated with Non-Small Cell Lung Cancer. PMID: 28872922 Skp2-mediated degradation of Cygb was identified as the key mechanism for controlling its oscillating levels during the cell cycle. PMID: 28948618 FOXM1 may play a central role in the skp2-cdk1 loop driving tumor progression. PMID: 27684411 simvastatin also increased p21 and p27 expression in tumor sections by reducing Skp2 expression and inducing AMPK activation and STAT3 suppression in the same tumor tissues. PMID: 28230855 Structural mimicry by a bacterial AnkB to human Skp2 hijacks the host ubiquitin-proteasome system. PMID: 28111017 p27 and its cognate ubiquitin ligases, Skp2/KPC/Pirh2, are specifically involved in determining the clinical profiles of lung carcinomas. PMID: 28601655 direct interactions of MAGE-A11 with Skp2 and cyclin A regulate the substrate-specificity of Skp2-mediated protein degradation. PMID: 27720894 abnormal levels of Skp2 and p27(KIP1) have probably been involved in the pathogenesis of ADH and DCIS. Thus, Skp2 and p27(KIP1) may serve as important diagnosis markers PMID: 28514182 High SKP2 expression is associated with lung cancer. PMID: 28789966 our results revealed a novel mechanism in which EZH2 stability is regulated by SKP2 through the TRAF6-mediated and K63-linked ubiquitination, which contributes to elevated levels of H3K27me3 during prostate tumorigenesis and CRPC growth. PMID: 27869166 Data demonstrate that AMPKa2 protein levels are reduced in bladder cancer and that this reduction is correlated with an increase in SKP2 expression with a concomitant reduction in p27 protein levels. PMID: 27638620 SKP2 expression can inhibit radiation induced bystander effect of esophageal cancer cells. The mechanism may function, at least partly, through the regulation of Rad51 in the ability to repair DNA damage. PMID: 28178195 AMPK deficiency results in nuclear CARM1 decrease mediated in part by SKP2, contributing to autophagy dysfunction in the aged heart. PMID: 28315332 Higher expression of Skp2 correlates with lower expression of p27kip1 in gastric cancer tissues. PMID: 27572672 The suppression of Skp2 reduced the enzyme activities of MMP-2. PMID: 26874697 Data suggest that mternally expressed gene 3 (Meg3) long non-coding RNA and microRNA miR-3163 may coordinate suppression of translation of S-phase kinase associated protein 2 (Skp2) mRNA in non-small cell lung cancer (NSCLC) cells to inhibit cell growth. PMID: 26482610 Data suggest that SIRT2 may induce Skp2 deacetylation and subsequent degradation to abolish the effects of Skp2 on p27 to affect NSCLC cell growth. PMID: 26942878 High expression of SKP2 is associated with non-muscle invasive urothelial bladder carcinoma. PMID: 26932430 HDACIs effects on Skp2 protein posttranslational modifications and/or on its removal PMID: 26682002 miR-186 has a suppressive role in esophageal squamous cell carcinoma progression via SKP2-mediated pathway PMID: 26568291 Patients with breast cancer have an increased SKP2 level. Interference in SKP2 gene expression can inhibit breast cancer cell growth. PMID: 26345857 High expression of SKP2 is associated with Advanced Ovarian Cancer. PMID: 26320455 Results demonstrate that curcumin exerts its antitumor activity through inhibition of glioma cell Skp2 pathway. PMID: 26046466 TRUSS is a novel substrate of E3 ligase Skp2. PMID: 26038816 Overexpression of LKB1 and Skp2 is found in hepatocellular carcinoma patients and predicts poor survival outcomes. PMID: 25728766 The Skp2-mH2A1-CDK8 axis has a critical role in breast cancer development via dysregulation of the G2/M transition, polyploidy, cell growth dysregulation, and loss of tumor suppression. PMID: 25818643 the Skp2mediated degradation of p27kip1 was important in the proliferation of tumor cells. The present study, therefore, provided a molecular reference for the treatment of liver cancer. PMID: 25572801 Over-expression of Skp2 resulted in the increased cell growth and number of S phase cells in Skp2 transfected MCF-7 cells PMID: 26429528 Caffeic acid phenethyl ester induced cell cycle arrest and growth inhibition in prostate cancer cells via regulation of Skp2, p53, p21Cip1, and p27Kip1. PMID: 25788262 Particularly for TNBC associated with Skp2/LRP6 overexpression. PMID: 25358452

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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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