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Human Polyclonal PDCD6 Primary Antibody for WB - ABIN1881643
Abe, Miyakushi, Nagai, Norimatsu: Study of the factors affecting the photoelectrode characteristics of a perylene/phthalocyanine bilayer working in the water phase. in Physical chemistry chemical physics : PCCP 2008
Show all 4 Pubmed References
ALG-2 is predominantly localized to a specialized region of the endoplasmic reticulum (ER), called the ER exit site (ERES), through its interaction with Sec31A. Sec31A is an outer coat protein of coat protein complex II (COPII) and is recruited from the cytosol to the ERES to form COPII-coated transport vesicles
Up-regulation of miR-20a by HPV16 E6 exerted growth-promoting effects by targeting PDCD6 in cervical carcinoma cells.
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-.
ALG-2 binding to Scotin is strictly calcium dependent, indicating a role of this interaction in calcium signaling pathways
Ca2+-loaded ALG-2 bridges Alix and TSG101 as an adaptor protein.
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
inability of the two-residue shorter ALG-2 isoform to bind Alix
the alg2 binding site is one of the key determinants of the retention kinetics of Sec31A at endoplasmic reticulum exit sites
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.
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
ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex.
Lack of ALG-2, ALIX or Vps4B each prevents shedding, and repair of the injured cell membrane
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.
Alix and ALG-2 are new actors of the TNF-R1 pathway
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.
analysed the expression of ALG-2 in 7371 tumor tissue samples of various origin; most notably, ALG-2 was upregulated in mesenchymal tumors.
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
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.
MAP1B heavy chain has a unique binding site for a calcium-binding protein ALG-2.
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.
Results provide a better understanding of the target recognition mechanism and conformational change of SOUL in the interaction with ALG-2.
ALG2 regulates glioblastoma cell proliferation, migration and tumorigenicity.
Substitution of either L52 with Ala or F148 with Ser of ALG-2 caused loss of binding abilities to PLSCR3 lacking type 1 motif but retained those to PLSCR3 lacking type 2 motif
ALG-2 is physiologically dispensable for apoptotic responses (ALG-2 protein)
This gene encodes a calcium-binding protein belonging to the penta-EF-hand protein family. Calcium binding is important for homodimerization and for conformational changes required for binding to other protein partners. This gene product participates in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death. In mice deficient for this gene product, however, apoptosis was not blocked suggesting this gene product is functionally redundant. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is also located on the short arm of chromosome 5.
programmed cell death 6
, programmed cell death protein 6
, apoptosis-linked gene 2 protein
, probable calcium-binding protein ALG-2