Dim2, also known as TXNL4B, is a member of the DIM1 family. The Dim protein family is composed of two classes, Dim1and Dim2, which share a common thioredoxin-like fold. They were originally identified for their role in cell cycle progression and have been found to interact with Prp6, an essential component of the spliceosome, which forms the bridge of U4/U6.U5-tri-snRNP. In spite of their biological and structural similarities, Dim1 and Dim2 proteins differ in many aspects. Dim1 bears distinctive structural motifs responsible for its interaction with other spliceosome components. Dim2 forms homodimers and contains specific domains required for its interactions with partners. This originality suggests that although both proteins are involved in pre-mRNA splicing, they are likely to be involved in different biological pathways. Dim2 roduced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids and having a molecular mass of 21.1kDa. It is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Dim2 has a vital role in pro-mRNA splicing. Dim2 is required in cell cycle progression for S/G2 transition and interacts with PRPF6 subunit of the spliceosome.
Dipeptidase 1 (DPEP1) is a kidney membrane enzyme that belongs to the peptidase M19 family. DPEP1 is a homodimer and is inhibited by L-penicillamine. DPEP1 hydrolyzes a variety of dipeptides and is implicated in renal metabolism of glutathione and its conjugates. DPEP1 is responsible for hydrolysis of the beta-lactam ring of antibiotics; such as penem and carbapenem. DPEP1 may play an important role in the regulation of leukotriene activity. DPEP1 expression in cancer is significantly higher than that in normal tissue. However; DPEP1 expression decreased with pathological differentiation; lymph-node and distant metastasis.
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
Dickkopf-related protein 1(DKK-1), is a member of the dickkopf family. DKK1 secreted proteins with two cysteine-rich domains separated by a linker region. It antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. 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.
This gene encodes a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.
DKK3 (dickkopf related protein 3) is a member of the dickkopf-related family consisting of DKK1 , DKK2 , DKK3 and DKK4. It is a secreted protein , and also known as REIC (Reduced Expansion in Immortalized Cells). The DKK3 protein is proposed to function as a secreted tumor suppressor since it is downregulated in a number of cancer cells and prostate cancer tissue and may be a promising candidate molecule for therapeutic interference. DKK3 protein is also a negative regulator of beta-catenin and its downregulation contribute to an activation of the beta-catenin signaling pathway.
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