ASPH Human

Aspartate Beta-Hydroxylase Human Recombinant

Cat. No.

BT29106

Source

Escherichia Coli.

Synonyms

AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

Appearance

Sterile Filtered colorless solution.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (75-270 a.a.) and having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag and purified by conventional chromatography.

Product Specs

Introduction

ASPH, an enzyme involved in calcium homeostasis, hydroxylates Asp or Asn residues within EGF domains. The expression of ASPH is regulated by two promoters and undergoes extensive alternative splicing, resulting in a variety of ASPH protein isoforms. These isoforms share similar N-terminal regions but exhibit significant variations in their C-terminal domains, leading to distinct functional properties. The longest isoforms (a and f) possess a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain responsible for hydroxylating aspartic acid or asparagine residues in EGF domains of various proteins, including protein C, coagulation factors VII, IX, and X, and complement factors C1R and C1S. Other isoforms differ primarily in their C-terminal sequences, lack the hydroxylase domain, and some localize to the endoplasmic reticulum and sarcoplasmic reticulum.

Description

Recombinant human ASPH, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 217 amino acids (residues 75-270), has a molecular weight of 24.5 kDa, and includes a 20 amino acid His Tag. Purification is achieved through standard chromatographic techniques.

Physical Appearance

A sterile, colorless solution.

Formulation

The ASPH protein solution is formulated in 20mM Tris-HCl (pH 8.0), 1mM DTT, and 10% glycerol.

Stability

For short-term storage (2-4 weeks), the product should be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal long-term stability, adding a carrier protein (0.1% HSA or BSA) is advised. Repeated freezing and thawing cycles should be avoided.

Purity

Purity is determined to be greater than 90.0% using SDS-PAGE analysis.

Synonyms

AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT.

Product Science Overview

Introduction

Aspartate Beta-Hydroxylase (ASPH) is a type II transmembrane protein that plays a crucial role in the post-translational modification of specific aspartyl and asparaginyl residues in epidermal growth factor-like domains (EGFDs) of target proteins. This enzyme is highly conserved and is part of the alpha-ketoglutarate-dependent dioxygenase family, which is essential for collagen biosynthesis.

Structure and Function

ASPH is an approximately 86 kDa protein located on the luminal side of the endoplasmic reticulum (ER). It hydroxylates the β-carbons of specific aspartyl and asparaginyl residues in the presence of ferrous iron. Unlike canonical EGFD disulfide patterns, ASPH catalyzes noncanonical EGFD substrates. The gene encoding ASPH is located at position q12.1 on human chromosome 8.

Biological Role

ASPH is widely expressed in proliferating placenta trophoblastic cells and is almost undetectable in normal adult tissues. However, its expression is significantly upregulated in various human malignancies, where it is associated with poor survival and prognosis. ASPH contributes to tumor cell migration, infiltration, and metastasis by enhancing cell proliferation, migration, and invasion. It also promotes tumor growth by stimulating angiogenesis and immunosuppression, primarily through the activation of Notch and SRC signaling pathways .

Clinical Significance

Due to its role in malignant transformation, ASPH has become a target for cancer therapy. Small molecule inhibitors of ASPH enzymatic activity have shown anti-metastatic effects in preclinical mouse models. Additionally, ASPH can be targeted by monoclonal antibodies and has been used as a tumor-associated antigen to induce both CD8+ and CD4+ T cells in mice. The PAN-301-1 vaccine against ASPH has already been tested in a phase 1 clinical trial in patients with prostate cancer.

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ASPH Human

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