Recombinant Human Programmed Cell Death Protein 6 (PDCD6) Protein (GST)

Name: Recombinant Human Programmed Cell Death Protein 6 (PDCD6) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08439P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Programmed Cell Death Protein 6 (PDCD6) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O75340
Target Symbol	PDCD6
Synonyms	AIP1; ALG 2; ALG-2-interacting protein 1; ALG2; ALIX; Apoptosis linked gene 2; Apoptosis linked gene 2 protein; Apoptosis-linked gene 2 protein; FLJ42309; FLJ46208; Hp95; KIAA1375; MA 3; MA3; MGC111017; MGC119050; MGC9123; PDCD 6; Pdcd6; PDCD6_HUMAN; PEF 1B; PEF1B; Probable calcium binding protein ALG 2; Probable calcium binding protein ALG2; Probable calcium-binding protein ALG-2; Programmed cell death 6; Programmed cell death 6-interacting protein; Programmed cell death protein 6; PS 2; PS2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV
Expression Range	1-191aa
Protein Length	Full Length
Mol. Weight	48.9kDa
Research Area	Apoptosis
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	Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes. Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes. Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats. In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification. Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Promotes localization and polymerization of TFG at endoplasmic reticulum exit site. Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis. May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. Its role in apoptosis may however be indirect, as suggested by knockout experiments. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway. In case of infection by HIV-1 virus, indirectly inhibits HIV-1 production by affecting viral Gag expression and distribution.; Has a lower Ca(2+) affinity than isoform 1.
Subcellular Location	Endoplasmic reticulum membrane; Peripheral membrane protein. Cytoplasmic vesicle, COPII-coated vesicle membrane. Cytoplasm. Nucleus. Endosome.
Database References	HGNC: 8765 OMIM: 601057 KEGG: hsa:10016 STRING: 9606.ENSP00000264933 UniGene: PMID: 29710555 the t(5;21)(p15;q22) translocation could be identified only when what had seemed like a del(21)(qq) in G-banded preparations was examined using FISH and RNA-sequencing directed at finding out what lay behind the 21q-. PMID: 29672642 ALG-2 binding to Scotin is strictly calcium dependent, indicating a role of this interaction in calcium signaling pathways PMID: 17889823 found that targeting Requiem and Alg-2 did not result in extended culture viability, but resulted in an increase in maximum viable cell numbers and cumulative IVCD under fed-batch conditions PMID: 20571937 the alg2 binding site is one of the key determinants of the retention kinetics of Sec31A at endoplasmic reticulum exit sites PMID: 20834162 This is the first report showing interaction of ALG-2 with a P-body component (PATL1).PATL1 as well as DCP1A, a well-known P-body marker, co-localized with a subset of ALG-2. PMID: 22437941 ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex. PMID: 24069399 Results show the crystal structure of the complex between ALG-2 and a peptide of Sec31A and found that the peptide binds to the third hydrophobic pocket (Pocket 3) and that ALG-2 recognizing 2 types of motifs at different hydrophobic surfaces of Sec31A. PMID: 25667979 These results indicate that ALG-2 has an anti-apoptotic function in HeLa cells by facilitating the passage through checkpoints in the G2/M cell cycle phase. PMID: 19013425 analysed the expression of ALG-2 in 7371 tumor tissue samples of various origin; most notably, ALG-2 was upregulated in mesenchymal tumors. PMID: 19383317 ALG-2/Sec31A interactions were not required for the localization of Sec31A to ER exit sites per se but appeared to acutely regulate the stability and trafficking of the cargo receptor p24 and the distribution of the vesicle tether protein p115 PMID: 25006245 Our study demonstrates that ALG-2 plays a role in the regulation of cytoskeletal rearrangement that drives cell polarization and migration in breast cancer cells. PMID: 27926525 MAP1B heavy chain has a unique binding site for a calcium-binding protein ALG-2. PMID: 29432744 These results suggest that a change in the intracellular calcium level plays a role in regulation of the secretory pathway via interaction of ALG-2 with MISSL and MAP1B. PMID: 28864773 The gene copy numbers and mRNA levels for both ALG-2 and HEBP2 are significantly upregulated in breast and lung cancer. Coexpression of ALG-2 and HEBP2 markedly increases the cytoplasmic pool of ALG-2 and alters the subcellular distribution of HEBP2. Abnormalities in the ALG-2/HEBP2 interaction impairs spindle orientation and positioning during mitosis. PMID: 28004381 The results suggest that ALG-2 acts as a Ca2+-sensitive adaptor to concentrate and polymerize TFG at endoplasmic reticulum exit sites, supporting a potential role for ALG-2 in COPII-dependent trafficking from the endoplasmic reticulum. PMID: 27813252 ALG2 has a tumor suppressive role in glioblastoma and might be a potential target for the treatment of glioblastoma. PMID: 28300556 miR-183 may function as an oncogene and may enhance cell proliferation by targeting PDCD6, implying a potential therapeutic target for this malignancy. PMID: 27738758 Achieved results show that polymorphism rs3756712 is signifi cantly associated with the risk of endometriosis development in Slovak women. Polymorphism rs4957014 did not show any connection with development of endometriosis PMID: 27546697 Our results suggest that PDCD6 may play an important role in the pathogenesis of cervical squamous cell carcinoma PMID: 25362542 PDCD6 may represent a biomarker candidate gene that could help to identify a group of patients at high risk for recurrence and death. PMID: 24792888 Palmitoylation sites and the N-terminal Pro-rich region were necessary for efficient secretion, but ABSs (ALG-2-binding sites) were dispensable. PMID: 23350699 The present study provided evidence that rs4957014 and rs3756712 are associated with Uterine leiomyoma (UL) risk, the results indicated that genetic polymorphisms in PDCD6 may contribute to the development of UL. PMID: 23551056 CHERP and ALG-2 participate in regulation of alternative splicing of IP3R1 pre-mRNA and provide new insights into post-transcriptional regulation of splicing variants in Ca(2+) signaling pathways. PMID: 24078636 the binding of ALG-2 to IST1 is Ca(2+)-dependent PMID: 23649269 the current study indicates that PDCD6 gene may be a new susceptibility gene to endometriosis. PMID: 23137875 The results of this study show that rs4957014G/T is associated with an increased risk of non-small cell lung cancer (NSCLC), which suggest that PDCD6 gene single nucleotide polymorphism is a risk factor for susceptibility of NSCLC. PMID: 23167403 we conclude that a novel p53-responsive gene PDCD6 is accumulated in the nucleus and induces apoptosis in response to DNA damage. PMID: 22712728 PDCD6 seems to play an important role in ovarian cancer progression. PMID: 22369209 PDCD6 exerts its anti-tumor potency by activating the p53-p21 protein for G1 phase of cell cycle progression and apoptosis PMID: 22142513 PDCD6 may have a role in advanced gastric cancer PMID: 22161137 programmed cell death 6 protein plays a significant role in modulating cellular angiogenesis PMID: 21893193 ALG-2 is stabilized by dimerization through its fifth EF-hand region PMID: 11883899 Pro/Gly/Tyr/Ala-rich hydrophobic region in Anexin XI masked the Ca(2+)-dependently exposed hydrophobic surface of ALG-2. PMID: 11883939 The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner. PMID: 12445460 ALG-2 has roles in both cell proliferation and cell death. PMID: 12445461 Data show that ALG-2 is overexpressed in liver and lung neoplasms, and is mainly found in epithelial cells in the lung. PMID: 12819013 The down-regulation of ALG-2 in human uveal melanoma cells compared to their progenitor cells, normal melanocytes, may provide melanoma cells with a selective advantage by interfering with Ca+-mediated apoptotic signals, thereby enhancing cell survival. PMID: 15366927 Raf-1 may mediate its anti-apoptotic function by interrupting ASK1-dependent phosphorylation of ALG-2. PMID: 15925322 ALG-2 is recruited to endoplasmic reticulum exit sites via Ca(2+)-dependent interaction with Sec31A and in turn stabilizes the localization of Sec31A at these sites. PMID: 16957052 ALG-2 alone evenly distributed within the cell, whereas in the presence of RBM22 the two proteins co-localized within the nucleus. PMID: 17045351 These findings establish Sec31A as a novel target for ALG-2 and provide a framework for studies on the roles of ALG-2 in ER-Golgi transport. PMID: 17196169 Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants PMID: 18256029 lower mRNA expression levels of PDCD6 were correlated significantly with a poor overall survival in gastric cancer. PMID: 18957060 Results describe the crystallization and structural analysis of N-terminally truncated human ALG-2. PMID: 18997320 ALG-2 acts as a Ca(2+) sensor that modulates the function of MCOLN1 along the late endosomal-lysosomal pathway. PMID: 19864416 Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. PMID: 11606059

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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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