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The protein encoded by SEC23A is a member of the SEC23 subfamily of the SEC23/SEC24 family. Additionally we are shipping SEC23A Proteins (4) and many more products for this protein.
Showing 10 out of 35 products:
Human Polyclonal SEC23A Primary Antibody for IP, WB - ABIN493432
Yanai, Saito, Kakinuma, Kon, Hirota, Taniguchi-Yanai, Nishijo, Shigematsu, Horiguchi, Kasuya, Sugiyama, Yagami, Murakami, Fukamizu: Renin-dependent cardiovascular functions and renin-independent blood-brain barrier functions revealed by renin-deficient mice. in The Journal of biological chemistry 2000
Show all 3 references for ABIN493432
Mouse (Murine) Polyclonal SEC23A Primary Antibody for ELISA, ICC - ABIN4352399
Bi, Mancias, Goldberg: Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. in Developmental cell 2007
ALG-2 (show PDCD6 Antibodies) attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A (show SEC31A Antibodies) complex.
Hypomorphic mutations of SEC23B (show SEC23B Antibodies) gene account for mild phenotypes of congenital dyserythropoietic anemia type II.
show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER
Data indicate that a synthetic polypeptide containing the N terminus of bovine AE1 (show SLC4A1 Antibodies) bound the Sec23A-Sec24C (show SEC24C Antibodies) complex through a selective interaction with Sec24C (show SEC24C Antibodies).
the BBF2H7 (show CREB3L2 Antibodies)-mediated Sec23A pathway is required for ER-to-Golgi procollagen trafficking to promote collagen synthesis
Sec23A overexpression reduced cell growth but did not induce apoptosis, whereas inhibition of Sec23A stimulated cell proliferation
When entering into mitosis, the COPII component Sec24Cp is simultaneously deglycosylated and phosphorylated; however, Sec23A is not.
Sec23A mutation causes cranio-lenticulo-sutural dysplasia, and disrupts the nucleation of COPII coat proteins at endoplasmic reticulum exit sites.
Data show that coupling of the Sec23/24 and Sec13 (show SEC13 Antibodies)/31 layers of the COPII coat is required to drive export of collagen from the endoplasmic reticulum, and that efficient COPII assembly is essential for normal craniofacial development during embryogenesis.
sec23b (show SEC23B Antibodies) is an essential component of the cartilage extracellular matrix secretory pathway in chondrocytes
results suggest that mammalian SEC23A and SEC23B (show SEC23B Antibodies) transport overlapping yet distinct spectra of cargo in vivo
Sec23a contains consensus TFII-I (show GTF2I Antibodies) binding sites in the proximal promoters; the chromatin immunoprecipitation analysis showed that TFII-I (show GTF2I Antibodies) transcription factors are recruited to these sites in vivo in Williams-Beuren syndrome.
Regulation of endoplasmic reticulum stress response by a BBF2H7 (show CREB3L2 Antibodies)-mediated Sec23a pathway is essential for chondrogenesis.
The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family. It is part of a protein complex and found in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. This protein has similarity to yeast Sec23p component of COPII. COPII is the coat protein complex responsible for vesicle budding from the ER. The encoded protein is suggested to play a role in the ER-Golgi protein trafficking.
SEC23-related protein A
, Sec23 homolog A (S. cerevisiae)
, protein transport protein Sec23A
, Sec23 homolog A
, COP-II coat subunit
, protein transport protein Sec23A-like