Recombinant Human Aspartyl/Asparaginyl Beta-Hydroxylase (ASPH) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04480P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ASPH.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ASPH.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ASPH.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ASPH.

Recombinant Human Aspartyl/Asparaginyl Beta-Hydroxylase (ASPH) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04480P
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Product Overview

Description Recombinant Human Aspartyl/Asparaginyl Beta-Hydroxylase (ASPH) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q12797
Target Symbol ASPH
Synonyms ASPH; BAHAspartyl/asparaginyl beta-hydroxylase; EC 1.14.11.16; Aspartate beta-hydroxylase; ASP beta-hydroxylase; Peptide-aspartate beta-dioxygenase
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence FDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPDT
Expression Range 75-270aa
Protein Length Partial of Isoform 6
Mol. Weight 38.2kDa
Research Area Signal Transduction
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.; membrane-bound Ca(2+)-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.
Subcellular Location [Isoform 1]: Endoplasmic reticulum membrane; Single-pass type II membrane protein.; [Isoform 4]: Sarcoplasmic reticulum membrane; Single-pass type II membrane protein.; [Isoform 8]: Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Protein Families Aspartyl/asparaginyl beta-hydroxylase family
Database References

HGNC: 757

OMIM: 600582

KEGG: hsa:444

STRING: 9606.ENSP00000368767

UniGene: PMID: 29580991

  • the hydroxylase activity of ASPH affected HCC metastasis through interacting with vimentin and regulating EMT. As such, ASPH might be a promising therapeutic target of HCC. PMID: 29764768
  • Higher levels of HAAH/humbug mRNA were found in the hepatocellular carcinoma tissues relative to the adjacent cancerfree tissue. PMID: 25394783
  • this study provides evidence that ASPH is mutated in a distinct form of syndromic ectopia lentis. PMID: 24768550
  • Data show that junctate (ASPH) is an interacting partner of Orai1-STIM1 complex. PMID: 22586105
  • Ca(2+) and JNT-dependent disassembly of the CSQ2 polymer PMID: 22123818
  • Aspartyl-asparaginyl-beta-hydroxylase is an important, positive regulator of trophoblastic cell motility, and it's inhibition in vivo leads to impaired implantation and fetal growth, and alters Notch-signaling mechanisms. PMID: 21862239
  • Low expression of AAH in the endochylema and nucleus of trephocyte may play a role in patients with missed abortion. PMID: 19197126
  • role of gene in neuroblastoma cell motility PMID: 12118090
  • AAH over-expression may contribute to the infiltrative growth pattern of cholangiocarcinoma cells by promoting motility. PMID: 12713872
  • junctate has a role in calcium homeostasis in eukaryotic cells PMID: 15302852
  • This review summarizes recent progress in elucidating the molecular mechanisms of hypoxia-inducible factor (HIF)-1 activation, focusing on the role of oxygen-dependent prolyl hydroxylase in hypoxia signal transduction. PMID: 16154531
  • Overexpression of aspartyl beta-hydroxylase plays a role in the development and progression of hepatocellular carcinoma. PMID: 16341145
  • enhanced AAH gene activity is a common feature of human hepatocellular carcinoma and growth factor signaling through IRS-1 regulates AAH expression and increases cell motility and invasion PMID: 16564107
  • Human aspartyl (asparaginyl) beta-hydroxylase (HAAH) mRNA is overexpressed in biliary cancer cell lines and possibly involved in the pathogenesis of bile duct cancer. PMID: 16673309
  • Abundant AAH expression in trophoblasts as well as in decidua and endometrial glands, with reduced expression in spontaneous abortion and small-for-gestational-age term deliveries, suggesting that AAH may serve as a biomarker of impaired implantation. PMID: 16949909
  • Study demonstrates that high levels of humbug immunoreactivity in colon carcinomas correlate with histologic grade and tumor behavior, suggesting that humbug can serve as a prognostic biomarker. PMID: 17020779
  • AAH and Humbug are over-expressed in SH-Sy5y neuroblastoma cells, and their mRNAs are regulated by insulin/IGF-1 signaling through Erk MAPK, PI3 kinase-Akt, and Cdk-5, which are known mediators of cell migration. PMID: 17156427
  • Expression analysis showed that the mRNA expression level of humbug was correlated with invasive potential in various human gastric cancer cell lines. PMID: 18288418
  • USF1 and USF2 positively regulate the core of P1 promoter od AAH. PMID: 19087304
  • High levels of aspartyl (asparaginyl)-beta-hydroxylase/humbug correlate with poor prognosis in non-small cell lung cancer, particularly squamous cell carcinoma subtype. PMID: 19200576
  • analysis of aspartyl (asparaginyl) beta-hydroxylase monoclonal antibodies PMID: 19663697
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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