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Mouse Anti-ASPH Recombinant Antibody (A10) (CBMAB-1152-CN)


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Published Data
Mouse Anti-ASPH Recombinant Antibody (A10) CBMAB-1152-CN in WB
Specific ASPH siRNAs visibly downregulate ASPH expression after 18 h. ...View More
Benelli, R., Costa, D., Mastracci, L., Grillo, F., Olsen, M. J., Barboro, P., ... & Ferrari, N. (2020). Aspartate-β-hydroxylase: a promising target to limit the local invasiveness of colorectal cancer. Cancers, 12(4), 971.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
A10
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA, IHC-P

Basic Information

Immunogen
Amino acids 382-681 mapping within an internal region of ASPH of human origin.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
aspartate beta-hydroxylase
Introduction
This gene is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. ASPH is thought to play an important role in calcium homeostasis. Alternative splicing of this gene results in five transcript variants which vary in protein translation, the coding of catalytic domains, and tissue expression.
Entrez Gene ID
444
UniProt ID
Q12797
Alternative Names
AAH; BAH; HAAH; JCTN; FDLAB; junctin; CASQ2BP1
Function
Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.
Isoform 8: membrane-bound Ca2+-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells.
Biological Process
Activation of cysteine-type endopeptidase activity Source: BHF-UCL
Activation of store-operated calcium channel activity Source: UniProtKB
Calcium ion homeostasis Source: UniProtKB
Calcium ion transmembrane transport Source: UniProtKB
Cellular response to calcium ion Source: UniProtKB
Detection of calcium ion Source: BHF-UCL
Ion transmembrane transport Source: Reactome
Muscle contraction Source: ProtInc
Peptidyl-aspartic acid hydroxylation Source: GO_Central
Positive regulation of calcium ion transport into cytosol Source: UniProtKB
Positive regulation of intracellular protein transport Source: UniProtKB
Positive regulation of proteolysis Source: BHF-UCL
Positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
Positive regulation of transcription, DNA-templated Source: UniProtKB
Regulation of cardiac conduction Source: Reactome
Regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
Regulation of cell communication by electrical coupling Source: BHF-UCL
Regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: UniProtKB
Regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
Regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
Response to ATP Source: UniProtKB
Cellular Location
Isoform 1: Endoplasmic reticulum membrane
Isoform 4: Sarcoplasmic reticulum membrane
Isoform 8: Endoplasmic reticulum membrane
Involvement in disease
Facial dysmorphism, lens dislocation, anterior segment abnormalities, and spontaneous filtering blebs (FDLAB): A syndrome characterized by dislocated crystalline lenses and anterior segment abnormalities in association with a distinctive facies involving flat cheeks and a beaked nose. Some affected individuals develop highly unusual non-traumatic conjunctival cysts (filtering blebs).
Topology
Cytoplasmic: 1-53 aa
Helical: 54-74 aa
Lumenal: 75-758 aa
More Infomation

Nagaoka, K., Ogawa, K., Ji, C., Cao, K. Y., Bai, X., Mulla, J., ... & Huang, C. K. (2021). Targeting aspartate beta-hydroxylase with the small molecule inhibitor MO-I-1182 suppresses cholangiocarcinoma metastasis. Digestive Diseases and Sciences, 66, 1080-1089.

Senthil, S., Sharma, S., Vishwakarma, S., & Kaur, I. (2021). A novel mutation in the aspartate beta-hydroxylase (ASPH) gene is associated with a rare form of Traboulsi syndrome. Ophthalmic Genetics, 42(1), 28-34.

Kanwal, M., Smahel, M., Olsen, M., Smahelova, J., & Tachezy, R. (2020). Aspartate β-hydroxylase as a target for cancer therapy. Journal of Experimental & Clinical Cancer Research, 39(1), 1-12.

Zheng, W., Wang, X., Hu, J., Bai, B., & Zhu, H. (2020). Diverse molecular functions of aspartate β‑hydroxylase in cancer. Oncology Reports.

Benelli, R., Costa, D., Mastracci, L., Grillo, F., Olsen, M. J., Barboro, P., ... & Ferrari, N. (2020). Aspartate-β-hydroxylase: A promising target to limit the local invasiveness of colorectal cancer. Cancers, 12(4), 971.

Barboro, P., Benelli, R., Tosetti, F., Costa, D., Capaia, M., Astigiano, S., ... & Ferrari, N. (2020). Aspartate β-hydroxylase targeting in castration-resistant prostate cancer modulates the NOTCH/HIF1α/GSK3β crosstalk. Carcinogenesis, 41(9), 1246-1252.

Nagaoka, K., Bai, X., Ogawa, K., Dong, X., Zhang, S., Zhou, Y., ... & Wands, J. R. (2019). Anti-tumor activity of antibody drug conjugate targeting aspartate-β-hydroxylase in pancreatic ductal adenocarcinoma. Cancer letters, 449, 87-98.

Holtzman, N. G., Lebowitz, M. S., Koka, R., Baer, M. R., Malhotra, K., Fuller, S. A., ... & Emadi, A. (2018). Aspartate Beta-Hydroxylase (ASPH) As a Novel Therapeutic Target in Acute Myeloid Leukemia. Blood, 132, 5273.

Huang, C. K., Iwagami, Y., Zou, J., Casulli, S., Lu, S., Nagaoka, K., ... & Wands, J. R. (2018). Aspartate beta-hydroxylase promotes cholangiocarcinoma progression by modulating RB1 phosphorylation. Cancer letters, 429, 1-10.

Zou, Q., Hou, Y., Wang, H., Wang, K., Xing, X., Xia, Y., ... & Shen, F. (2018). Hydroxylase activity of ASPH promotes hepatocellular carcinoma metastasis through epithelial-to-mesenchymal transition pathway. EBioMedicine, 31, 287-298.

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For research use only. Not intended for any clinical use.

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