Human DKK3 Protein (DKK-HM403)

  • Express System: HEK293
  • Product Tag: C-His-Avi
  • Purity: > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
  • Exact Sequence: Pro23-Ile350

Catalog: DKK-HM403

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Product Description Recombinant Human DKK3 Protein is expressed from HEK293 with His tag and Avi tag at the C-Terminus.It contains Pro23-Ile350.

Product Background

Dkk-3, also known as REIC (Reduced Expansion in Immortalized Cells), is one of four numbered members of the Dickkopf family of Wnt antagonists.DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease.

Product Category

Recombinant Protein

Target

DKK3
Synonyms Dickkopf-3; Dkk3; REIC; REICdkk-3; RIG; RIG-like 5-6; RIG-like 7-1; AW061014; C87148

Gene/Protein ID

Q9UBP4

Species

Human

Exact Sequence

Pro23-Ile350
Molecular Weight The protein has a predicted MW of 39.5 kDa. Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result.

Product Tag

C-His-Avi

Express System

HEK293
Purity > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
Endotoxin Less than 1EU per ug by the LAL method.
Form Lyophilized
Shipping Shipped at ambient temperature.
Formulation Lyophilized from 0.22um filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Reconstitution Centrifuge the tube before opening. Reconstituting to a concentration more than 100 ug/ml is recommended. Dissolve the lyophilized protein in distilled water.
Stability And Storage Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
The purity of Human DKK3 is greater than 95% as determined by SEC-HPLC.
Human DKK3 on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.

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