Recombinant Human Dna-Binding Protein Inhibitor Id-2 (ID2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10231P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Dna-Binding Protein Inhibitor Id-2 (ID2) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10231P
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Product Overview

Description Recombinant Human Dna-Binding Protein Inhibitor Id-2 (ID2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q02363
Target Symbol ID2
Synonyms bHLHb26; Cell growth inhibiting gene 8; class B basic helix loop helix protein 26; Class B basic helix-loop-helix protein 26; DNA binding protein inhibitor ID 2; DNA binding protein inhibitor ID2; DNA-binding protein inhibitor ID-2; GIG 8; GIG8; Helix loop helix protein ID2 ; ID2; ID2_HUMAN; ID2A; ID2H; Inhibitor of differentiation 2; Inhibitor of DNA binding 2; Inhibitor of DNA binding 2, dominant negative helix loop helix protein; MGC26389
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG
Expression Range 1-134aa
Protein Length Full Length
Mol. Weight 30.9kDa
Research Area Epigenetics And Nuclear Signaling
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 Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Restricts the CLOCK and ARNTL/BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism.
Subcellular Location Cytoplasm. Nucleus.
Database References
Tissue Specificity Highly expressed in early fetal tissues, including those of the central nervous system.

Gene Functions References

  1. Results show that self-assembly decreases the backbone flexibility of ID2 protein regions: helix-loop-helix (HLH) and the nuclear export signal (NES), that are important for interaction with basic-HLH transcription factors or for nucleocytoplasmic shuttling. PMID: 29642431
  2. the results of the present study suggest that lncRNA H19 regulates the expression of ID2 through competitive binding to hsamiR19a and hsamiR19b, which may serve a role in acute myelocytic leukemia cell proliferation. PMID: 28765931
  3. ID2 is localized to peritoneal mesothelial and stromal cells of women with and without endometriosis. ID2 mRNA expression is lower in peritoneum adjacent to the endometriosis lesions compared to distal sites PMID: 27385728
  4. The ID2 gene expression was increased in the most advanced stage of endometriosis and in ovarian endometriomas. Considering that the genes studied participate either directly or indirectly in cellular processes that can lead to cell migration, angiogenesis, and inappropriate invasion, it is possible that the deregulation of these genes caused the development and maintenance of ectopic tissue. PMID: 28678915
  5. Data indicate that the expression level of ID2 in GBM cells can predict the sensitivity of GBM-derived tumor cells to decreased glucose levels. PMID: 28206987
  6. Results show that ID2 signaling was involved in BMP4-induced hepatocellular carcinoma proliferation and that Id2 was directly upregulated by BMP4, resulting in the mediated expression of cell cycle regulatory protein of CDKN1B. PMID: 28543546
  7. EYA4 functions as tumor suppressor gene in pancreatic ductal adenocarcinoma via repressing beta-catenin/ID2 activation, and was an independent prognostic factor in PDAC. PMID: 27378242
  8. Results show that MLL-AF9 reduces Id2 and increases E2-2 expression to drive and sustain leukemia stem cell potential in MLL-rearranged acute myeloid leukemia (AML). Low expression of Id2 or of an Id2 gene signature is associated with poor prognosis in not only MLL-rearranged but also t(8;21) AML patients. PMID: 27374225
  9. We further demonstrated, for the first time, that the degree of hypoxia-induced CSC-sphere formation (CD44(+) subpopulation) in vitro and of tumor metastasis/dissemination in vivo were markedly suppressed by knocking down Id2 expression PMID: 26965643
  10. ID2 knockdown triggers important changes in cell behavior, that is, it significantly reduces the expression of N-cadherin, vimentin and Snail, induces E-cadherin expression and leads to a more differentiated phenotype exemplified by changes in cell shape. ID2 therefore represents a potential therapeutic target during salivary gland cancer progression PMID: 27364596
  11. cell invasion drastically increased with increased expression and activity of MMP2. Immunoprecipitation revealed a direct interaction between ID2 and zinc finger transcription factor, snail family transcriptional repressor 1 (SNAIL1) PMID: 27807072
  12. High Id2 expression is associated with Neuroblatoma. PMID: 25771836
  13. ID2 binds to the VHL ubiquitin ligase complex, displaces VHL-associated Cullin 2, and impairs HIF2alpha ubiquitylation and degradation PMID: 26735018
  14. Downregulation of the Id2 gene by RNAi could increase the chemosensitivity of glioblastoma cells. Id2 could be a good molecular target for glioblastoma gene therapy. PMID: 25773386
  15. role of Id2-TGFbeta crosstalk in reversible adaptive plasticity in neuroblastoma PMID: 24376712
  16. Importantly, the distinct ID2 expression patterns in acute leukemias (AL) indicate a specific deregulation of ID2 in the various types of AL and may support subtyping of AL. PMID: 24292846
  17. ID2 was involved in cancer cell responses to Arsenic Tri-Oxide (ATO). Increased expression of ID2 was found in cancer cells following ATO treatment. In addition, specific silencing of ID2 enhanced cell apoptosis induced by ATO treatment. PMID: 25076250
  18. study shows that Id2, Id3 and Id4 are each able to overcome TGF-beta dependence, and establish a role for Ids as key mediators of TGF-beta melanomagenesis PMID: 24343358
  19. Id2 overexpression in neural stem cells is associated with inhibition of the Notch effector Hey1 and glioma formation in the brains of mice. PMID: 24425046
  20. PreBII large cells in adults, but not in children, showed highly upregulated expression of the differentiation inhibitor, inhibitor of DNA binding 2 (ID2), in absence of changes in expression of the ID2-binding partner E2A. PMID: 23825313
  21. A reduction in Id2 is critical for transforming growth factor (TGF)beta1-induced alpha-SMA expression in renal proximal tubule epithelial cells but is not sufficient in it self to induce alphaSMA (smooth muscle actin) even in the context of reduced E-cadherin. PMID: 23320068
  22. ID2 expression affects the susceptibility hepatoma cell lines to an HDAC inhibitor by regulating the expression of anti-apoptotic genes. PMID: 23403953
  23. Id2 induces squamous cell carcinoma tumor growth and proliferation through the NF-kappaB/cyclin D1 pathway. PMID: 22835384
  24. Higher ID2 expression was associated with advanced breast cancer. PMID: 23645773
  25. upregulated H19 increases bladder cancer growth by regulating ID2 expression PMID: 23399020
  26. Data indicate that ID2.K47A, ID2.Q55A and ID3.R52A, ID3.R60A had wildtype like expression levels in E. coli. PMID: 23119064
  27. preliminary X-ray data analysis of the human ID2 homodimer PMID: 23143248
  28. A critical role of Id2 is revealed in the control of effector CD4 T cell population size and the development of T helper (Th) cell type 17-mediated autoimmune encephalomyelitis. PMID: 22745378
  29. ID2 in nucleus was increased in nasopharyngeal carcinoma when compared with that in normal nasopharynx tissues. Higher expression level of nuclear ID2 was significantly associated with tumor size, lymph node metastasis, and clinical stage. PMID: 22551584
  30. Id2 mutations do not seem to be involved in ureteropelvic junction obstruction. PMID: 21927809
  31. Id2 and Id4 regulated glioblastoma multiforme neurosphere differentiation through downregulating of another bHLH family member, the oligodendroglial lineage-associated transcription factors (Olig) 1 and 2 PMID: 22380883
  32. This review reported that ID2 protein is a negative transcription factor regulating oligodendroglia differentiation. PMID: 22253220
  33. Findings indicate that Id2 functions as a proproliferative gene that antagonizes p53-mediated cell cycle regulation in NPCs and may contribute to the malignant proliferation of glioma-derived tumor stem cells. PMID: 21608079
  34. Large scale RNAi screen reveals that the inhibitor of DNA binding 2 (ID2) protein is repressed by p53 family member p63 and functions in human keratinocyte differentiation. PMID: 21478550
  35. AMP-activated protein kinase (PRKAA1/2, aka AMPK) mediates the stress-induced proteasome-dependent loss of ID2 at high stress levels. PMID: 20876741
  36. expression of vFLIP decreased the expression levels of Id2 and Id3 as well as cyclin E and cyclin A compared with the vFLIP-null cells PMID: 20512523
  37. ID2 can interact with the canonical clock components CLOCK and BMAL1 and mediate inhibitory effects on mPer1 expression PMID: 20861012
  38. T cell development is impaired by Id2, most likely by sequestering HEB, whereas NK cell development is promoted by increasing a pool of CD1a-CD5+ NK cell progenitors, which together with IL-15 differentiate into mature NK cells PMID: 20483740
  39. VEGF165 may partially inhibit TGF-beta1-induced epithelial-mesenchymal transition by upregulating the expressions of BMP-7 and Id2. PMID: 19180920
  40. Metastatic tumor cells overexpress c-myc, leading to upregulation of Id2 expression; the aberrantly elevated amount of Id2 represses SEMA3F expression and, as a consequence, enhances the ability of tumor cells to migrate and invade. PMID: 20388805
  41. Hypoxia-induced ID-2 may contribute to joint destruction in rheumatoid arthritis patients by promoting synovial fibroblast-dependent osteoclastogenesis. PMID: 19950294
  42. Id2 is critical for cellular proliferation and is the oncogenic effector of N-myc in human neuroblastoma. PMID: 11782392
  43. determination as a novel target of transcriptional activation by EWS-ETS fusion proteins in Ewing family tumors PMID: 12447693
  44. upregulation is mediated by the chimeric EWS/ets protein in Ewing sarcoma PMID: 12527902
  45. We found no correlation between MYCN and ID2 expression in neuroblastoma cell lines or tumor specimens. However, we did find a significant positive correlation between MYC and ID2 expressions in both MYCN-amplified and single-copy tumor specimens PMID: 12545167
  46. Id2 is up-regulated during dendritic cells development in vitro and crucial for the development of distinct dendritic cells subsets in vivo PMID: 12598895
  47. Transcriptional regulation of ID2 by the MycN oncoprotein is unlikely to be a seminal molecular event resulting in a highly malignant neuroblastoma phenotype. PMID: 12670915
  48. Mad expression and Id2 down-regulation are important events during the TGF-beta cytostatic program in epithelial cells. PMID: 12824180
  49. The decreased level of Id2 was associated with growth suppression and does support the prevalent conception of the action of Id2 as a stimulator of cell growth PMID: 14582708
  50. ID-2 appears to act as an important protein for the maintenance of a differentiated and noninvasive phenotype in normal and transformed breast cells. PMID: 14612502

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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.

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