ASPH
ASPH (aspartate beta-hydroxylase, also known as BAH, JCTN, HAAH and CASQ2BP1) is a membrane-bound, calcium-sensing protein of the endoplasmic and sarcoplasmic reticulum. Its longest isoforms also carry a hydroxylase domain that modifies EGF-like domains in other proteins. Browse Assay Genie's current range of ASPH research reagents below, or read on for the biology behind the target.
ASPH is a membrane-bound Ca(2+)-sensing protein and a structural component of the ER-plasma membrane junctions. One isoform, isoform 8, regulates the activity of Ca(2+) release-activated Ca(2+) (CRAC) channels in T-cells. The NCBI Gene summary describes the ASPH gene as thought to play an important role in calcium homeostasis.
The ASPH gene is expressed from two promoters and undergoes extensive alternative splicing. The resulting proteins share varying amounts of overlap near their N-termini but differ substantially in their C-terminal domains, which gives them distinct functional properties. The longest isoforms, a and f, include a C-terminal aspartyl/asparaginyl beta-hydroxylase domain. This domain hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of certain proteins, including protein C, coagulation factors VII, IX and X, and the complement factors C1R and C1S.
Other isoforms differ mainly in their C-terminal sequence and lack the hydroxylase domain. Some of these have been localised to the endoplasmic and sarcoplasmic reticulum, where they are found in complexes with calsequestrin, triadin and the ryanodine receptor and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis. The protein belongs to the aspartyl/asparaginyl beta-hydroxylase family, and HGNC places the gene in the aspartate beta-hydroxylase domain containing group. The mouse ortholog is Asph.
ASPH is thought to play an important role in calcium homeostasis and acts as a membrane-bound Ca(2+)-sensing protein.
ASPH is a structural component of ER-plasma membrane junctions, making it relevant to studies of membrane contact sites.
Isoform 8 regulates the activity of Ca(2+) release-activated Ca(2+) channels in T-cells, linking ASPH to calcium signalling in immunity.
Some ASPH isoforms have been implicated in metastasis, so the gene is of interest in studies of cancer progression.
ASPH is a membrane-bound Ca(2+)-sensing protein that is a structural component of ER-plasma membrane junctions. Its longest isoforms also have a hydroxylase domain that hydroxylates aspartic acid or asparagine residues in EGF-like domains. Shorter isoforms lack this domain and regulate calcium release from the sarcoplasmic reticulum.
ASPH is also known as aspartyl/asparaginyl beta-hydroxylase, CASQ2BP1, BAH, JCTN and HAAH. The gene is expressed from two promoters and extensively spliced. Isoforms a and f are the longest and contain the hydroxylase domain, while other isoforms differ mainly in their C-terminal sequence.
The mouse ortholog is called Asph, so rodent models can be used for functional work. Per the NCBI Gene summary, some ASPH isoforms have been implicated in metastasis. Check the datasheet of any product for its validated reactivity.
Other calcium-handling proteins, hydroxylases and ER membrane proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q12797; product specifications from Assay Genie datasheets.