Recombinant Human Neuroglobin (NGB) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04338P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Neuroglobin (NGB) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04338P
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Product Overview

Description Recombinant Human Neuroglobin (NGB) 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 Q9NPG2
Target Symbol NGB
Synonyms Neuroglobin; NGB; NGB_HUMAN
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MERPEPELIRQSWRAVSRSPLEHGTVLFARLFALEPDLLPLFQYNCRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLASLGRKHRAVGVKLSSFSTVGESLLYMLEKCLGPAFTPATRAAWSQLYGAVVQAMSRGWDGE
Expression Range 1-151aa
Protein Length Full Length
Mol. Weight 32.9kDa
Research Area Transport
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 Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.
Subcellular Location Perikaryon. Cytoplasm. Mitochondrion.
Protein Families Globin family
Database References

HGNC: 14077

OMIM: 605304

KEGG: hsa:58157

STRING: 9606.ENSP00000298352

UniGene: PMID: 30041403

  • This study demonstrated that serum NGB levels were significantly associated with 6-month unfavorable outcomes, indicating that Ngb can play a role in predicting 6-month unfavorable outcomes. PMID: 29738858
  • Results show that the expression of NGB in glioma is grade related and is negatively regulated at the transcriptional level by PPARgamma suggesting an important role of NGB in glioma progression. PMID: 28410531
  • The authors demonstrate that Glu53, Glu60, and Glu118 of human Ngb are crucial for both the neuroprotective activity and interaction with Gi. Moreover, they show that Lys46, Lys70, Arg208, Lys209, and Lys210 residues of Gi are important for binding to human Ngb. PMID: 27109834
  • Ngb-H64Q-CCC binds CO about 500 times more strongly than hemoglobin, which could be useful in detecting and eliminating carbon monoxide poisoning PMID: 27928027
  • these results highlight the involvement of ERa activation and of E2/ERa-dependent NGB upregulation in the insensitivity of MCF-7 to paclitaxel. These novel findings could have important implications in the development of targeted therapeutics for overcoming paclitaxel insensitivity in ERa-positive human breast cancer PMID: 27312786
  • Knockdown of GATA-2 caused NGB expression to drop dramatically, indicating GATA-2 as an essential transcription factor for the activation of NGB expression via binding to a novel distal regulatory element of NGB. PMID: 27651453
  • analysis of how the interaction of hydrogen sulfide with human neuroglobin is muted by a distal ligand PMID: 28246171
  • NO oxidation kinetics at physiological NO concentrations. The use of a polarized electrode to efficiently interconvert the ferric (Fe(3+)) and ferrous (Fe(2+)) forms of an immobilized NGB showed that the disulfide bridge both defines the kinetics of NO dioxygenase activity and regulates appearance of the free ferrous deoxy-NGB, which is the redox active form of the protein in contrast to oxy-NGB. PMID: 27402851
  • Taken together, this work support the first evidence that Ngb can be potentially used as a promising biomarker and target for novel treatment of human glioma PMID: 28103511
  • The cochlear nuclei and superior olivary complex (SOC) also express considerable amounts of Ngb. Within the human SOC, many medial superior olive neurons, and scattered neurons in the LSO, were Ngb-immunoreactive PMID: 25636685
  • Study characterized the presence of Ngb in the human cochlea PMID: 26556771
  • Findings suggest a control model for neuroglobin's anti-apoptotic activity under physiological conditions. While in normoxic conditions, its activity is maintained at low level, an immediate transition to an hypoxic situation increases it drastically. PMID: 26305249
  • The review summarizes the recent experimental findings, mainly focusing on the mechanisms of Ngb's protection and induction during ischemic/hypoxic conditions and it roles in astrocytes, tumors, as well as in neurite outgrowth. [review] PMID: 25372753
  • Neuroglobin player role in estrogen receptor alpha-positive cancer cell viability. PMID: 25299774
  • a mechanism for redox control of human Ngb (hNgb) activity PMID: 24855999
  • 17beta-estradiol-induced NGB up-regulation could act as an oxidative stress sensor, which does not oppose to the pro-apoptotic 17beta-estradiol effect in ER beta-containing colon cancer cells unless a rise of oxidative stress occurs. PMID: 25683270
  • first X-ray structure of wild-type human neuroglobin is reported at 1.74 A resolution PMID: 24699645
  • Glu60 of human Ngb is a crucial residue for its GDI and neuroprotective activities PMID: 24376733
  • Data show that chimeric neuroglobin and myoglobin were generated by swapping a regulatory segment. PMID: 25452214
  • This paper for the first time presents the data on neuroglobin distribution in human cerbellum using immunohistochemistry. PMID: 25552092
  • Findings indicate that myoglobin (Mb) and neuroglobin (Ngb) can be expressed in nonmuscle and non-neural contexts. PMID: 24446190
  • analysis of single nucleotide polymorphisms in neuroglobin that affect transcription and possibly Alzheimer's Disease PMID: 24362753
  • Neuroglobin brain levels are increased in Alzheimer's disease patients compared to controls. PMID: 23648513
  • These findings suggest that neuroglobin is expressed early in the course of neuronal differentiation and may, therefore, have a role in neurodevelopment. PMID: 23643985
  • NGB is expressed in the carotid body of heroin addicts and may have a role in compensating for the negative effects of heroin PMID: 23319379
  • Ngb and Cygb are expressed in the solitary tract nucleus and in the carotid body, and may have roles in the processing of cardiovascular and respiratory reflex inputs PMID: 23835959
  • Report neuroglobin expression in human brain. PMID: 23160832
  • functional impact of heme disorder and cysteine oxidation state on the properties of the Ngb ligand PMID: 23135388
  • the oxidative stress-induced structural changes of human Ngb are essential for its neuroprotective activity. PMID: 22787149
  • We found that NGB was present in a rat astrocytoma cell line (C6), human astrocytoma cell line (U251), and human astrocytoma tissues PMID: 22009023
  • overexpression in non-small cell lung cancer is associated with histological subtype, hypoxia PMID: 21601304
  • 14-3-3 binding and phosphorylation of neuroglobin during hypoxia modulate six-to-five heme pocket coordination and rate of nitrite reduction to nitric oxide PMID: 21965683
  • The phenylalanine B10 residue of neuroglobin plays a key role in transmitting the structural information from the disulfide bridge to the heme-pocket region. PMID: 21704585
  • This review describes the discovery of neuroglobin over a decade ago, its structure, affinity for oxygen, and its expression in cerebral neurons, all of which suggest it plays a role in providing oxygen to the brain. PMID: 21620833
  • Caenorhabditis elegans globin GLB-26 (expressed from gene T22C1.2) has been studied in comparison with human neuroglobin (Ngb) and cytoglobin (Cygb) for its electron transfer properties PMID: 21674044
  • This study demonistrated that Neuroglobin overexpression in brain with arteriovenous malformation and intracerebral hemorrhage. PMID: 21725774
  • Cimeric Myoglobin has a cell-membrane-penetrating activity similar to zebrafish Ngb. PMID: 21304818
  • Data suggest a potential role of DNA methylation in regulating NGB tissue-specific expression. PMID: 21362510
  • neuroglobin may function as a physiological oxidative stress sensor and a post-translationally redox-regulated nitrite reductase that generates NO under six-to-five-coordinate heme pocket control PMID: 21296891
  • There is a plausible central role for neuroglobin in the control of apoptosis. PMID: 21190290
  • A significant association was found between Alzheimer disease risk and a variant in the NGB gene. Data is consistent with a model where women, older individuals and carriers of specific genotypes have lower levels of NGB leading to increased risk for AD. PMID: 19010568
  • Ngb may confer protection against ischemia-reperfusion injury in the brain through its intrinsic antioxidant properties. PMID: 20571522
  • These data favor the hypothesis that the disulfide bond between Cys46 and Cys55 modulates the functioning of human neuroglobin. PMID: 20643048
  • the haplotype block represented by rs3783988 in neuroglobin appears to influence recovery after severe traumatic brain injury PMID: 20345238
  • These data provides an explanation the action of neuroglobin in the protection of nerve cells from unwanted apoptosis. PMID: 20091232
  • The acid-induced denaturation pathway of apo-Ngb can be illustrated from the native state (N), via a partially unfolded state (U(A)) to the molten globule state (MG). PMID: 20227336
  • Ischemic stroke increases the expresssion of the neuroprotective protein neuroglobin in brain. PMID: 20075359
  • The conformational and functional stability of Ngb at acidic pH was analyzed. PMID: 19860834
  • Full-length cDNA cloning and genomic organization of NGB have been reported. PMID: 11820779

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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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