Recombinant Human Hepatoma-Derived Growth Factor (HDGF) Protein (His)

Name: Recombinant Human Hepatoma-Derived Growth Factor (HDGF) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00189P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Human Hepatoma-Derived Growth Factor (HDGF) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P51858
Target Symbol	HDGF
Synonyms	(HDGF)(High mobility group protein 1-like 2)(HMG-1L2)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL
Expression Range	1-240aa
Protein Length	Full Length
Mol. Weight	33.7 kDa
Research Area	Cancer
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	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	HGNC: 4856 OMIM: 600339 KEGG: hsa:3068 STRING: 9606.ENSP00000357189 UniGene: Hs.743948
Tissue Specificity	Ubiquitous.

Gene Functions References

miR139 was downregulated in epithelial ovarian cancer, and acted as a tumor suppressor by directly targeting HDGF. PMID: 28713954
high serum levels of HDGF were significantly correlated to bone metastasis and poorer prognosis of non-small cell lung cancer. PMID: 28592712
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
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
functional diversity of HDGF isoforms PMID: 27926477
our findings first indicate that the interaction of HDGF and beta-catenin may play a crucial role in tumorigenesis of synovial sarcoma. PMID: 26842923
HDGF was overexpressed in hepatocellular carcinoma patients and cells. PMID: 27273265
miRNA497 directly targets hepatomaderived growth factor (HDGF) in prostate cancer cells. PMID: 26780929
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
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
HDGF and beta-catenin interact as a positive feedback loop, which plays an important role in carcinogenesis and progression of colorectal carcinoma. PMID: 26296979
HDGF is important in promoting malignant biological behaviors, including proliferation, migration and invasion of hilar cholangiocarcinoma cells. PMID: 26081074
Hepatoma-derived growth factor overexpression is involved in liver carcinogenesis. PMID: 25938538
Meta-analysis results provide evidence that HDGF may be a new indicator of poor cancer prognosis. PMID: 25773828
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
HDGF overexpression is common in early-stage cervical adenocarcinoma. PMID: 25421244
The expression level of hepatoma-derived growth factor (HDGF) significantly decreased in response to the virus-associated RNAs under replication-deficient condition. PMID: 25275311
HDGF can promote IHCC cells progression, including proliferation, invasion, and angiogenesis PMID: 25262276
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
These data suggested that irradiated fibroblasts promoted invasion, growth, EMT and HDGF expression of ESCC. PMID: 25677618
The expression of nuclear HDGF might be closely related to the carcinogenesis, clinical biological behaviors, and prognosis of gallbladder adenocarcinoma. PMID: 25071353
HDGF is a potential unfavorable factor for the progression and prognosis of endometrial carcinoma. PMID: 24692842
Data indicate that hepatoma-derived growth factor (HDGF) was a target of miR-195 in non-small cell lung cancer (NSCLC) cells. PMID: 24891187
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
ADAM9 high expression is correlated positively and significantly with HDGF high expression in non-small cell lung cancer. PMID: 24770635
Patients with higher HDGF and CD31 expression level had poorer overall survival rates. PMID: 23771798
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
Combining p53 expression and HDGF expression significantly improved prognostic stratification for patients with Ewing family tumor. PMID: 24072730
Together, these results indicate that HDGF downregulation participates in POMC-induced suppression of metastasis and EMT in melanoma. PMID: 23468531
Suggest that HDGF exhibits oncogenic properties and may be a novel prognostic factor in Ewing's sarcoma. PMID: 23878072
Up-regulation of hepatoma-derived growth factor facilities tumor progression in malignant melanoma. PMID: 23536873
The suppressive effect of miR-16 on cell proliferation, colony formation, migration, and invasion is partially mediated by inhibiting HDGF expression. PMID: 23954293
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
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
Expression of a cytosolic variant of hepatoma-derived growth factor causes a redistribution of nucleolin into the cytoplasm. PMID: 23305559
Hepatoma-derived growth factor regulates breast cancer cell invasion by modulating epithelial--mesenchymal transition. PMID: 22247069
Hepatoma-derived growth factor overexpression contributes to the oncogenic processes in oral cancer cells PMID: 22361040
Differential proteomic analysis of human glioblastoma and neural stem cells reveals HDGF as a novel angiogenic secreted factor PMID: 22331796
High hepatoma-derived growth factor is associated with gliomas. PMID: 22037800
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
found that HDGF was overexpressed also in primary gastric, breast, and lung cancer tissues harboring mutant p53 genes PMID: 22006999
HDGF was highly expressed in 158 non-small cell lung cancer tissues compared with normal control. PMID: 21426662
High HDGF is associated with hilar cholangiocarcinoma. PMID: 20848225
Increased nuclear expression of HDGF is a potential unfavourable prognostic factor for patients with hepatoma-derived growth factor PMID: 21255068
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
High hepatoma-derived growth factor is associated with colorectal carcinoma. PMID: 19924574
results suggest that HDGF is involved in cell growth, cell invasion, and apoptosis PMID: 21302807
The present study is aimed at examining the role of HDGF in keloid pathogenesis. PMID: 19432814
HDGF expression is upgraded in postoperative stage I non-small cell lung cancer patients, and is a significantly independent predictive factor. PMID: 18478933
Hepatoma-derived growth factor stimulates cell growth after translocation to the nucleus PMID: 11751870

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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.