ASPH Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q12797 |
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Clone Names | 100318100 |
Gene ID | 444 |
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Other Names | Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, ASP beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASPH, BAH |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | ASPH |
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Synonyms | BAH |
Function | [Isoform 1]: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. |
Cellular Location | [Isoform 1]: Endoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28056} [Isoform 8]: Endoplasmic reticulum membrane; Single-pass type II membrane protein |
Tissue Location | Isoform 1 is detected in all tissues tested. Isoform 8 is mainly expressed in pancreas, heart, brain, kidney and liver. Isoform 8 is expressed in kidney (at protein level) |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene is thought to play an important role in calciumhomeostasis. The gene is expressed from two promoters and undergoesextensive alternative splicing. The encoded set of proteins sharevarying amounts of overlap near their N-termini but havesubstantial variations in their C-terminal domains resulting indistinct functional properties. The longest isoforms (a and f)include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domainthat hydroxylates aspartic acid or asparagine residues in theepidermal growth factor (EGF)-like domains of some proteins,including protein C, coagulation factors VII, IX, and X, and thecomplement factors C1R and C1S. Other isoforms differ primarily inthe C-terminal sequence and lack the hydroxylase domain, and somehave been localized to the endoplasmic and sarcoplasmic reticulum.Some of these isoforms are found in complexes with calsequestrin,triadin, and the ryanodine receptor, and have been shown toregulate calcium release from the sarcoplasmic reticulum. Someisoforms have been implicated in metastasis.
References
Xue, T., et al. Hybridoma (Larchmt) 28(4):251-257(2009)Luu, M., et al. Hum. Pathol. 40(5):639-644(2009)Finotti, A., et al. BMC Mol. Biol. 9, 110 (2008) :Beausoleil, S.A., et al. Proc. Natl. Acad. Sci. U.S.A. 101(33):12130-12135(2004)Treves, S., et al. J. Cell Biol. 166(4):537-548(2004)
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