Mouse Anti-STT3A Recombinant Antibody (CBYY-I0909) (CBMAB-I2077-YY)

Basic Information
Formulations & Storage [For reference only, actual COA shall prevail!]
Target
N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity).
STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A (PubMed:19167329).
Biological Process post-translational protein modificationManual Assertion Based On ExperimentIBA:GO_Central
Biological Process protein N-linked glycosylationManual Assertion Based On ExperimentIDA:ComplexPortal
Biological Process protein N-linked glycosylation via asparagineManual Assertion Based On ExperimentIMP:UniProtKB
Endoplasmic reticulum membrane
A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
Congenital disorder of glycosylation 1W, autosomal dominant (CDG1WAD):
A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. CDG1WAD patients show variable skeletal anomalies, short stature, macrocephaly, and dysmorphic features. Some have impaired intellectual development. Additional features include increased muscle tone and muscle cramps.
Helical: 18-38
Lumenal: 39-119
Helical: 120-138
Cytoplasmic: 139-140
Helical: 141-158
Lumenal: 159-169
Helical: 170-189
Cytoplasmic: 190-191
Helical: 192-206
Lumenal: 207-211
Helical: 212-228
Cytoplasmic: 229-233
Helical: 234-259
Lumenal: 260-267
Helical: 268-287
Cytoplasmic: 288-300
Helical: 301-321
Lumenal: 322-356
Helical: 357-379
Cytoplasmic: 380-385
Helical: 386-402
Lumenal: 403-406
Helical: 407-428
Cytoplasmic: 429-453
Helical: 454-473
Lumenal: 474-705
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Please try the standard protocols which include: protocols, troubleshooting and guide.
Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols
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Custom Antibody Labeling
We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).
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