Recombinant Human Programmed Cell Death 6-Interacting Protein (PDCD6IP) Protein (His)

Name: Recombinant Human Programmed Cell Death 6-Interacting Protein (PDCD6IP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07340P
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 Programmed Cell Death 6-Interacting Protein (PDCD6IP) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8WUM4
Target Symbol	PDCD6IP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	PAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEV
Expression Range	402-652aa
Protein Length	Partial
Mol. Weight	32.3 kDa
Research Area	Cell Biology
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	Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. May play a role in the regulation of both apoptosis and cell proliferation. Regulates exosome biogenesis in concert with SDC1/4 and SDCBP. By interacting with F-actin, PARD3 and TJP1 secures the proper assembly and positioning of actomyosin-tight junction complex at the apical sides of adjacent epithelial cells that defines a spatial membrane domain essential for the maintenance of epithelial cell polarity and barrier.; (Microbial infection) Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function requires the interaction with CHMP4B. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as enveloped virus budding (HIV-1 and other lentiviruses).
Subcellular Location	Cytoplasm, cytosol. Melanosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Secreted, extracellular exosome. Cell junction, tight junction. Midbody, Midbody ring.
Database References	HGNC: 8766 OMIM: 608074 KEGG: hsa:10015 STRING: 9606.ENSP00000411825 UniGene: PMID: 27578500 Alix acts in concert with endophilin A to promote clathrin-independent endocytosis of cholera toxin and to regulate cell migration. PMID: 27244115 Revealed the transition of diffuse ALIX protein signals into a multivesicular body-like pattern during adenoma-carcinoma sequence in colorectal neoplasms. PMID: 27150162 Alix plays an important role in the proliferation of glioma cells and overexpression in gliomas predicts poor survival. PMID: 26980041 ALIX regulates P2Y1 degradation. PMID: 27301021 farnesylation of K-Ras was required for its packaging within extracellular nanovesicles, yet expressing a K-Ras farnesylation mutant did not decrease the number of nanovesicles or the amount of Alix protein released per cell. PMID: 27909058 These findings indicate that Alix binds to Ago2 and miRNAs, suggesting that it plays a key role in miRNA enrichment during extracellular vesicles biogenesis. PMID: 26935291 The authors find that HIV-1 nucleocapsid mimics the PDZ domains of syntenin, a membrane-binding adaptor involved in cell-to-cell contact/communication, to capture the Bro1 domain of ALIX, which is an ESCRTs recruiting cellular adaptor. PMID: 26962944 We found that ARRDC3 is required for ALIX ubiquitination induced by activation of PAR1 PMID: 26490116 phosphorylation of the intramolecular interaction site in the PRD is one of the major mechanisms that activates the ESCRT function of ALIX PMID: 26859355 homologous domain of human Bro1 domain-containing proteins, Alix and Brox, binds CHMP4B but not STAM2, despite their high structural similarity PMID: 26866605 Accordingly, ALIX depletion leads to furrow regression in cells with chromosome bridges, a phenotype associated with abscission checkpoint signaling failure. PMID: 26929449 Findings indicate that the PDCD6IP 15bp insertion/deletion polymorphism decreases the risk of breast neoplasm in an Iranian population. PMID: 26063962 The serum lever of Alzheimer's disease were decrease and the expression of ALIX strongly correlated with the Mini-Mental State Examination scores of the AD patients PMID: 25502766 our findings identify heparanase as a modulator of the syndecan-syntenin-ALIX pathway, fostering endosomal membrane budding and the biogenesis of exosomes by trimming the heparan sulfate chains on syndecans PMID: 25732677 Our data reveal that AIP1, by inhibiting VEGFR2-dependent signaling in tumor niche, suppresses tumor EMT switch, tumor angiogenesis, and tumor premetastatic niche formation to limit tumor growth and metastasis. PMID: 26139244 Lack of ALG-2, ALIX or Vps4B each prevents shedding, and repair of the injured cell membrane PMID: 25534348 Alix is critically involved in multivesicular body sorting of membrane receptors in mammalian cells. PMID: 25510652 Aip1 has a role in actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring PMID: 25451933 ALIX is recruited to the neck of the assembling HIV-1 virion and is mostly recycled after virion release. PMID: 24834918 Results suggest that programmed cell death 6 interacting protein (PDCD6IP) insertion/deletion polymorphism was potentially related to non-small cell lung cancer (NSCLC) susceptibility in Chinese Han population. PMID: 24870593 HIV-1 Nef interacts with Alix in late endosomes, and this is required for efficient lysosomal targeting of CD4. PMID: 25118280 Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2. PMID: 24637612 Alix protein plays a critical role in the maintenance of the barrier function of T84 monolayers PMID: 24712823 ALIX regulates these mammalian cell-specific cytokinesis, exosome release, and virus budding. [Review] PMID: 24287454 The results of in vitro binding assays using purified recombinant proteins indicated that ALG-2 functions as a Ca(2)-dependent adaptor protein that bridges ALIX and ESCRT-I to form a ternary complex PMID: 23924735 Common genetic variations in PDCD6IP may influence hepatocellular carcinoma risk, possibly through promoter activity-mediated regulation. PMID: 23777424 Alix serves as an adaptor that allows human parainfluenza virus type 1 to interact with the host cell ESCRT system. PMID: 23527201 Lysobisphosphatidic acid recruits ALIX onto late endosomes via the calcium-bound Bro1 domain, triggering a conformational change in ALIX to mediate the delivery of viral nucleocapsids to the cytosol during infection. PMID: 23664863 Data indicate that AP-3 facilitates PAR1 interaction with ALIX. PMID: 22833563 study reports that the V domain of ALIX binds directly and selectively to K63-linked polyubiquitin chains, exhibiting a strong preference for chains composed of more than three ubiquitins PMID: 23201121 BFRF1 recruits the ESCRT components to modulate nuclear envelope for the nuclear egress of Epstein Barr virus. PMID: 22969426 At the midbody, BRCA2 influences the recruitment of endosomal sorting complex required for transport (ESCRT)-associated proteins, Alix and Tsg101, and formation of CEP55-Alix and CEP55-Tsg101 complexes during abscission. PMID: 22771033 Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG-2-interacting protein X (Alix PMID: 22641034 Identify key role for syndecan-syntenin-ALIX in membrane transport and signalling processes. PMID: 22660413 structural analysis of the Bro1 domain protein BROX and functional analyses of the ALIX Bro1 domain in HIV-1 budding PMID: 22162750 Mutation of residues within the Phe105 loop of the Bro1 domain compromise Alix function in HIV-1 release. PMID: 21889351 Mutations designed to destabilize the closed conformation of the V domain opened the V domain, increased ALIX membrane association, and enhanced HIV-1 budding. PMID: 21715492 Data suggest that the boomerang-shaped Bro1 domain of Alix appears to escort hepatitis B virus naked capsids without ESCRT. PMID: 21129143 HIV-1 infection affects the expression of host factors TSG101 and Alix PMID: 21528537 The authors demonstrate that ALIX/AIP1, an ESCRT-associated host protein, is required for the incorporation of the nucleoprotein of Mopeia virus, a close relative of Lassa virus, into Z-induced virus-like particles (VLPs). PMID: 21248028 Crystal structures revealed that anchoring tyrosines and nearby hydrophobic residues contact the ALIX V domain, revealing how SIV gag proteins employ a diverse family of late-domain sequences to bind ALIX and promote virus budding. PMID: 20962096 studies on intramolecular interactions:the relieving of specific, autoinhibitory interactions within ALIX regulates binding with ESCRT proteins or viral proteins and is critical for ALIX to participate in retroviral budding PMID: 20929444 Examined changes in subcellular proteomes of different cellular compartments of human endothelial cells upon DENV2 infection. Double immunofluorescence staining revealed colocalization of Alix with late endosomal lysobisphosphatidic acid (LBPA). PMID: 20669987 Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X PMID: 20670214 inability of the two-residue shorter ALG-2 isoform to bind Alix PMID: 20691033 The results indicate YLDL motif in M protein is essential for efficient budding in the context of virus infection and suggest involvement of Alix/AIP1 in Sendai virus budding. PMID: 20605035 Together these data support a model in which Alix recruits Nedd4-1 to facilitate HIV-1 release mediated through the LYPX(n)L/Alix budding pathway via a mechanism that involves Alix ubiquitination. PMID: 20519395 p95 has roles in regulating cell adhesion and morphology. PMID: 12360406 AIP1/Alix interacts with the apoptosis-linked protein ALG-2 and recognizes recognize the protein-protein binding motif YPXL/I, where Tyr, Pro, and Leu/Ile are crucial for its interactive properties PMID: 12588984

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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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