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MAP1B (show MAP1B Proteins) heavy chain has a unique binding site for a calcium-binding protein (show CETN1 Proteins) 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 (show MAP1B Proteins).
The gene copy numbers and mRNA levels for both ALG-2 and HEBP2 (show HEBP2 Proteins) are significantly upregulated in breast and lung cancer. Coexpression of ALG-2 and HEBP2 (show HEBP2 Proteins) markedly increases the cytoplasmic pool of ALG-2 and alters the subcellular distribution of HEBP2 (show HEBP2 Proteins). Abnormalities in the ALG-2/HEBP2 (show HEBP2 Proteins) interaction impairs spindle orientation and positioning during mitosis.
The results suggest that ALG-2 acts as a Ca2 (show CA2 Proteins)+-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.
ALG2 has a tumor suppressive role in glioblastoma and might be a potential target for the treatment of glioblastoma.
miR (show MLXIP Proteins)-183 may function as an oncogene (show RAB1A Proteins) and may enhance cell proliferation by targeting PDCD6, implying a potential therapeutic target for this malignancy.
Our results suggest that PDCD6 may play an important role in the pathogenesis of cervical squamous cell carcinoma
PDCD6 may represent a biomarker candidate gene that could help to identify a group of patients at high risk for recurrence and death.
Palmitoylation sites and the N-terminal Pro-rich region were necessary for efficient secretion, but ABSs (ALG-2-binding sites) were dispensable.
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.
ALG2 regulates glioblastoma cell proliferation, migration and tumorigenicity.
Substitution of either L52 with Ala or F148 with Ser (show SIGLEC1 Proteins) of ALG-2 caused loss of binding abilities to PLSCR3 (show PLSCR3 Proteins) lacking type 1 motif but retained those to PLSCR3 (show PLSCR3 Proteins) 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