Human BANK1 Alexa Fluor® 350-conjugated Antibody Summary
Ser480-His785 (Cys650Arg)
Accession # Q8NDB2
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
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Preparation and Storage
Background: BANK1
BANK1 (B cell scaffold protein with ANKyrin repeats) is a cytoplasmic scaffold protein containing ankyrin repeats. Although its predicted MW is 85 kDa, due to its highly acidic nature, it runs anomalously at 97-105 kDa in SDS-PAGE. It is expressed in select cell types, including mature B cells and pancreatic islet beta ‑cells. In B cells, following BCR activation, IP3 is generated and BANK1 is phosphorylated by BCR-associated Syk (Spleen Tyr kinase). At this point, phosphorylated BANK1 subsequently interacts with both cytosolic Lyn (Lck/Yes-related Novel tyrosine kinase) and IP3R, leading to an IP3 receptor highly sensitive to IP3. Increased cellular IP3 binding to IP3R stimulates the release of calcium from intracellular stores. BANK1 is also posited to participate in the regulation of IgM production, its role in this case being that of a negative modulator of secretion. Human BANK1 is 785 amino acids (aa) in length. It contains an IP3R interaction region (aa 1-154), followed by a DBB domain (aa 200-327) that is involved in dimerization, and two consecutive ANK repeats (aa 345-408). There are at least three isoform variants. One utilizes an alternative start site at Met31, a second contains an eight aa substitution for aa 1-23, and a third shows a deletion of aa 24-156. BANK1 is known to form homo- and heterodimers with its isoforms, and a Arg61 to His61 transition is reported to be correlated with reduced homooligomer formation. Over aa 480-785, human BANK1 shares 73% aa sequence identity with mouse BANK1.
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