Recombinant Human HDGF Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0844NP
BL-0844NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-0844NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human HDGF Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0844NP
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Product Overview

Description Recombinant Human Hepatoma-Derived Growth Factor is produced by our E.coli expression system and the target gene encoding Met1-Tyr100 is expressed with a 6His tag at the C-terminus.
Accession P51858
Synonym Hepatoma-Derived Growth Factor; HDGF; High Mobility Group Protein 1-Kike 2; HMG-1L2; HDGF; HMG1L2
Gene Background Hepatoma-Derived Growth Factor is a original member of the HDGF family. HDGF is a cytoplasmic protein and contains one PWWP domain. HDGF expression levels are high in the nucleus and cytoplasm of smooth muscle and endothelial cells. HDGF has proliferative, angiogenic and neurotrophic activity. HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. As a heparin-binding protein, which is highly expressed in tumor cells where it stimulates proliferation. HDGF has mitogenic activity for fibroblasts and acts as a transcriptional repressor. It has been shown that HDGF is linked with tumorigenesis and the growth of cancer.
Molecular Mass 12.6 KDa
Apmol Mass 14 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 1mM DTT, 1mM EDTA, pH 7.5.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Acts as a transcriptional repressor. Has mitogenic activity for fibroblasts. Heparin-binding protein.; Does not have mitogenic activity for fibroblasts. Does not bind heparin.; Has mitogenic activity for fibroblasts. Heparin-binding protein.
Subcellular Location [Isoform 1]: Nucleus. Cytoplasm. Secreted, extracellular exosome.; [Isoform 2]: Nucleus. Cytoplasm. Secreted, extracellular exosome.; [Isoform 3]: Nucleus. Cytoplasm. Secreted, extracellular exosome.
Protein Families HDGF family
Database References
Tissue Specificity Ubiquitous.

Gene Functions References

  1. miR139 was downregulated in epithelial ovarian cancer, and acted as a tumor suppressor by directly targeting HDGF. PMID: 28713954
  2. high serum levels of HDGF were significantly correlated to bone metastasis and poorer prognosis of non-small cell lung cancer. PMID: 28592712
  3. Data suggested that HDGF knockdown inhibits cellular migration and invasion in vitro of prostate cancer via modulating epithelial-mesenchymal transition signaling pathway, as well as MMP2 and MMP9 signaling pathway. These results supported that HDGF is a relevant protein in the progression of prostate cancer and may serve as a potentially therapeutic target for prostate cancer as well as its downstream targets. PMID: 29300772
  4. HDGF is overexpressed in both androgen-sensitive and androgen-insensitive cell lines. Forced overexpression enhanced cell viability but knockdown reduced proliferation of benign prostate cells.Ectopic HDGF overexpression of HDGF in up-regulated cyclin E and BCL-2, but down-regulated BAX. Treatment with a HDGF monoclonal antibody and vitamin K2 reduced proliferation and inhibited NF-kB expression in a tumor cell line. PMID: 27692835
  5. functional diversity of HDGF isoforms PMID: 27926477
  6. our findings first indicate that the interaction of HDGF and beta-catenin may play a crucial role in tumorigenesis of synovial sarcoma. PMID: 26842923
  7. HDGF was overexpressed in hepatocellular carcinoma patients and cells. PMID: 27273265
  8. miRNA497 directly targets hepatomaderived growth factor (HDGF) in prostate cancer cells. PMID: 26780929
  9. describe two previously unknown HDGF isoforms, HDGF-B and HDGF-C, generated via alternative splicing with structurally unrelated N-terminal regions of their hath region PMID: 26845719
  10. study uncovers a novel function of HDGF as a messenger of cellular condition (alarmin) which in-turn modulates cellular function-aspects that could be used as a biomarker for ovarian cancer. PMID: 26612514
  11. HDGF and beta-catenin interact as a positive feedback loop, which plays an important role in carcinogenesis and progression of colorectal carcinoma. PMID: 26296979
  12. HDGF is important in promoting malignant biological behaviors, including proliferation, migration and invasion of hilar cholangiocarcinoma cells. PMID: 26081074
  13. Hepatoma-derived growth factor overexpression is involved in liver carcinogenesis. PMID: 25938538
  14. Meta-analysis results provide evidence that HDGF may be a new indicator of poor cancer prognosis. PMID: 25773828
  15. HDGF contains conserved N-terminal HATH domains with a characteristic structural motif, namely the PWWP motif. This study defines the role of the first residue of the PWWP motif in modulating HATH domain stability and oligomer formation in binding. PMID: 26067205
  16. HDGF overexpression is common in early-stage cervical adenocarcinoma. PMID: 25421244
  17. The expression level of hepatoma-derived growth factor (HDGF) significantly decreased in response to the virus-associated RNAs under replication-deficient condition. PMID: 25275311
  18. HDGF can promote IHCC cells progression, including proliferation, invasion, and angiogenesis PMID: 25262276
  19. Results suggest that HDGF downregulation significantly suppresses glioma cell proliferation, migration, invasion in vitro and tumorigenesis in vivo is probably involved in the activation of both the PI3K/Akt and the TGF-beta signaling pathways PMID: 24986090
  20. These data suggested that irradiated fibroblasts promoted invasion, growth, EMT and HDGF expression of ESCC. PMID: 25677618
  21. The expression of nuclear HDGF might be closely related to the carcinogenesis, clinical biological behaviors, and prognosis of gallbladder adenocarcinoma. PMID: 25071353
  22. HDGF is a potential unfavorable factor for the progression and prognosis of endometrial carcinoma. PMID: 24692842
  23. Data indicate that hepatoma-derived growth factor (HDGF) was a target of miR-195 in non-small cell lung cancer (NSCLC) cells. PMID: 24891187
  24. expression of HDGF was negatively correlated with miR-141 in gastric cancer tissues: the suppressive effects of miR-141 on GC cell proliferation, colony formation, in vitro migration, and invasion were partially mediated by suppressing HDGF expression. PMID: 24276755
  25. ADAM9 high expression is correlated positively and significantly with HDGF high expression in non-small cell lung cancer. PMID: 24770635
  26. Patients with higher HDGF and CD31 expression level had poorer overall survival rates. PMID: 23771798
  27. Positive expression of HDGF was detected in 46.2 % of patients with extrahepatic cholangiocarcinoma and correlated with poor tumor differentiation. The HDGF expression group had lower survival than the negative HDGF expression group. PMID: 23793608
  28. Combining p53 expression and HDGF expression significantly improved prognostic stratification for patients with Ewing family tumor. PMID: 24072730
  29. Together, these results indicate that HDGF downregulation participates in POMC-induced suppression of metastasis and EMT in melanoma. PMID: 23468531
  30. Suggest that HDGF exhibits oncogenic properties and may be a novel prognostic factor in Ewing's sarcoma. PMID: 23878072
  31. Up-regulation of hepatoma-derived growth factor facilities tumor progression in malignant melanoma. PMID: 23536873
  32. The suppressive effect of miR-16 on cell proliferation, colony formation, migration, and invasion is partially mediated by inhibiting HDGF expression. PMID: 23954293
  33. Studied HDGF in gallbladder cancer (GBC).Patients with nuclear HDGF-pos tumors had worse survival than patients with HDGF-negative tumors. Treatment of GBC-SD and SGC-996 lines with HDGF-siRNA significantly reduced the proliferation of GBC cell lines. PMID: 23609195
  34. Tumor samples from non-small cell lung cancers show an inverse relationship between microRNA-497 and HDGF levels, and ectopic expression of miR-497 significantly inhibited tumor growth and angiogenesis in a xenograft model PMID: 23673296
  35. Expression of a cytosolic variant of hepatoma-derived growth factor causes a redistribution of nucleolin into the cytoplasm. PMID: 23305559
  36. Hepatoma-derived growth factor regulates breast cancer cell invasion by modulating epithelial--mesenchymal transition. PMID: 22247069
  37. Hepatoma-derived growth factor overexpression contributes to the oncogenic processes in oral cancer cells PMID: 22361040
  38. Differential proteomic analysis of human glioblastoma and neural stem cells reveals HDGF as a novel angiogenic secreted factor PMID: 22331796
  39. High hepatoma-derived growth factor is associated with gliomas. PMID: 22037800
  40. The interactome suggests that HDGF is a multifunctional protein and participates in many cellular events, including ribosome biogenesis, RNA processing, DNA damage repair and transcriptional regulation. PMID: 21907836
  41. found that HDGF was overexpressed also in primary gastric, breast, and lung cancer tissues harboring mutant p53 genes PMID: 22006999
  42. HDGF was highly expressed in 158 non-small cell lung cancer tissues compared with normal control. PMID: 21426662
  43. High HDGF is associated with hilar cholangiocarcinoma. PMID: 20848225
  44. Increased nuclear expression of HDGF is a potential unfavourable prognostic factor for patients with hepatoma-derived growth factor PMID: 21255068
  45. High HDGF expression is associated with poor overall survival in patients with hepatocellular carcinoma. Down-regulation of HDGF inhibits the growth, anchorage-independent growth, migration and invasion of HepG2 cells. PMID: 20846397
  46. High hepatoma-derived growth factor is associated with colorectal carcinoma. PMID: 19924574
  47. results suggest that HDGF is involved in cell growth, cell invasion, and apoptosis PMID: 21302807
  48. The present study is aimed at examining the role of HDGF in keloid pathogenesis. PMID: 19432814
  49. HDGF expression is upgraded in postoperative stage I non-small cell lung cancer patients, and is a significantly independent predictive factor. PMID: 18478933
  50. Hepatoma-derived growth factor stimulates cell growth after translocation to the nucleus PMID: 11751870

FAQs

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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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