1. Recombinant Proteins
  2. Enzymes & Regulators
  3. Transferases (EC 2)
  4. DYRK1A Protein, Human

DYRK1A protein has dual serine/threonine and tyrosine kinase activities. DYRK1A Protein, Human is the recombinant human-derived DYRK1A protein, expressed by E. coli , with tag free. The total length of DYRK1A Protein, Human is 359 a.a., .

For research use only. We do not sell to patients.

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Description

DYRK1A protein has dual serine/threonine and tyrosine kinase activities. DYRK1A Protein, Human is the recombinant human-derived DYRK1A protein, expressed by E. coli , with tag free. The total length of DYRK1A Protein, Human is 359 a.a., .

Background

DYRK1A, a dual-specificity kinase endowed with both serine/threonine and tyrosine kinase activities, plays a pivotal role in various cellular processes. It exhibits a substrate preference for proline at position P+1 and arginine at position P-3, showcasing its specificity in substrate recognition. In the context of DNA damage response, DYRK1A emerges as a key participant in double-strand breaks repair, phosphorylating RNF169 to enhance its capability to impede TP53BP1 accumulation at DSB sites, thereby facilitating homologous recombination repair. Moreover, DYRK1A acts as a positive regulator of transcription by functioning as a CTD kinase, orchestrating the phosphorylation of the C-terminal domain of the large subunit of RNA polymerase II (POLR2A). This kinase may contribute to a signaling pathway governing nuclear functions related to cell proliferation and modulates alternative splicing through the phosphorylation of the splice factor SRSF6. With pro-survival functions, DYRK1A negatively regulates apoptosis, promoting cell survival under genotoxic stress by phosphorylating SIRT1, consequently inhibiting p53/TP53 activity. Additionally, DYRK1A targets SEPTIN4, SEPTIN5, and SF3B1 for phosphorylation at 'Thr-434,' further expanding its regulatory repertoire.

Species

Human

Source

E. coli

Tag

Tag Free

Accession

Q13627 (S127-E485)

Gene ID

1859

Molecular Construction
N-term
DYRK1A (S127-E485)
Accession # Q13627
C-term
Synonyms
DYRK1A; Dual specificity tyrosine-phosphorylation-regulated kinase 1A; Dual specificity YAK1-related kinase; HP86; Protein kinase minibrain homolog; MNBH; hMNB
Purity

Greater than 90% as determined by reducing SDS-PAGE.

Appearance

Solution.

Formulation

Supplied as a 0.22 μm filtered solution of 20mM HEPES (pH 7.5), 150 mM NaCl, 1mM TCEP.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

Please use rapid thawing with running water to thaw the protein.

Storage & Stability

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping

Shipping with dry ice.

Documentation

DYRK1A Protein, Human Related Classifications

Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

  • Reconstitution Calculator

  • Dilution Calculator

  • Specific Activity Calculator

The reconstitution calculator equation

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration
= ÷

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
× = ×
C1   V1   C2   V2

The specific activity calculator equation

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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Product Name:
DYRK1A Protein, Human
Cat. No.:
HY-P701667
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