Recombinant Mouse Glial Fibrillary Acidic Protein (GFAP) Protein (His-SUMO)

Name: Recombinant Mouse Glial Fibrillary Acidic Protein (GFAP) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03089P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) GFAP.

Collections: High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Mouse Glial Fibrillary Acidic Protein (GFAP) 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	P03995
Target Symbol	GFAP
Synonyms	GfapGlial fibrillary acidic protein; GFAP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MERRRITSARRSYASETVVRGLGPSRQLGTMPRFSLSRMTPPLPARVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKDSKQEHKDVVM
Expression Range	1-430aa
Protein Length	Full Length
Mol. Weight	65.9kDa
Research Area	Others
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	GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells.
Subcellular Location	Cytoplasm.
Protein Families	Intermediate filament family
Database References	KEGG: mmu:14580 STRING: 10090.ENSMUSP00000064691 UniGene: PMID: 28597341 These results indicate that autoantibodies against GFAP could serve as a predictive marker for the development of overt autoimmune diabetes. PMID: 28546444 GFAP is specifically expressed in the auricular chondrocytes, and assumes a pivotal role in resistance against mechanical stress. PMID: 28063220 compared open-skull and thinned-skull imaging methods for two-photon laser microscopy of live astrocytes in neocortex of GFAP-GFP transgenic mice PMID: 28107381 work reveals that an Alexander disease-causing mutation alters GFAP turnover kinetics in vivo and provides an essential foundation for future studies aimed at preventing or reducing the accumulation of GFAP. PMID: 28223355 Tat expression or GFAP expression led to formation of GFAP aggregates and induction of unfolded protein response (UPR) and endoplasmic reticulum (ER) stress in astrocytes. PMID: 27609520 Study provides evidence that transcription of one of the astrocyte-specific genes, Gfap, is cooperatively regulated by co-expressed genes and their regulatory factors. PMID: 27041678 This study demonstrated the GFAP-ApoE4 mice exhibited motor impairments when compared to GFAP-ApoE3 and wild-type mice. PMID: 26892275 PINK1 deficiency causes defects in GFAP-positive astrogliogenesis during brain development. PMID: 26746235 Gnasxl deficiency does not directly affect glial development in the hypothalamus, since it is expressed in neurons, and Gfap-positive astrocytes and tanycytes appear normal during early postnatal stages. PMID: 27080240 Induction of glial cytokine expression was sequential, aligned with active sickness behavior, and preceded increased Iba-1 or GFAP immunoreactivity after lipopolysaccharide challenge PMID: 26470014 Study provides a mechanistic link between the GFAP mutations/overexpression and the symptoms in those affected with Type II Alexander disease PMID: 26190408 Study described GFAP-expressing non-myelinating Schwann cells in the lung, validated a transgenic mouse line that drives expression of cre under a GFAP promoter PMID: 26442852 findings thus show that the inability to produce GFAP and Vim affects normal retinal physiology and that the effect of IF deficiency on retinal cell survival differs, depending on the underlying pathologic condition PMID: 26251181 CUL4B as a negative regulator of GFAP expression during neural development. PMID: 26025376 Astrocytes deficient of GFAP and vimentin showed decreased Notch signal sending competence and altered expression of Notch signaling pathway-related genes PMID: 26118771 Absence of GFAP, or both GFAP and vimentin, alters Alzheimer's disease-induced changes in gene expression profile of astrocytes, showing a compensation of the decrease of neuronal support genes and a trend for a higher inflammatory expression profile PMID: 25731615 Data indicate that glial fibrillary acidic protein (GFAP) was up-regulated in satellite glial cells (SGCs) in dorsal root ganglia 14 days after streptozotocin injection. PMID: 25312986 Findings demonstrate that ENT1 regulates GFAP expression and possibly astrocyte function PMID: 25365803 Data suggest that prenatal alterations in expression of various fetal brain proteins (including down-regulation of Gfap) are associated with aberrant behavioral characteristics of transgenic mice that model autism-like behavior. PMID: 25849768 Study shows that increased levels of astrocytic GFAP can contribute to increases on inter-ictal spikes but do not represent a risk factor for appearance of post-traumatic seizures, even when there is increase in reactive gliosis PMID: 25069089 The Phactr4 signals were not associated with F-actin fibers but were closely associated with intermediate filaments such as nestin and glial fibrillary acidic protein (GFAP) fibers. PMID: 24748504 Report increasing glial fibrillary acidic protein expression and electron microscopic features of brain edema in rodent cerebral malaria. PMID: 24966914 absence of GFAP and vimentin in glial cells does not seem to affect the outcome after peripheral motoneuron injury but may have an important effect on the response dynamics PMID: 24223940 the astrocyte became activated, exhibiting significantly increased levels of GFAP expression directly related to the level of HIV/VSV replication PMID: 24254728 traumatic scratch injury to astrocytes triggered a calcium influx from the extracellular compartment and activated the JNK/c-Jun/AP-1 pathway to switch on GFAP PMID: 24123203 Data show that CD8 T cells reactive to glial fibrillary acidic protein (GFAP), a protein expressed in astrocytes, drive unique aspects of inflammatory central nervous system autoimmunity. PMID: 24591371 Brain levels of GFAP and Tau proteins decreased significantly at 6 h and increased considerably at 24 h after repeated blast exposures. Plasma samples showed a similar initial decrease and later increase over this timeframe. PMID: 23933206 Data indicate that Gfapdelta is expressed in the in developing mouse brain sub-ventricular zones in accordance with the described localization in the developing and adult human brain. PMID: 23991052 GFAP was found to be downregulated in HSV-1 acute infection in cornea and upregulated in late stage, suggesting that GFAP might play some role during HSV-1 infection in cornea. PMID: 23758602 Data show that neurofibromatosis type 1 (NF1)-inactivation results in a cell-autonomous increase in glial fibrillary acidic protein+ (GFAP+), but not in NG2 proteoglycan NG2+, cell proliferation in vitro. PMID: 23318450 this study demonistrated that mouse models of Alexander disease exhibit significant pathology in GFAP-positive radial glia-like cells in the dentate gyrus, and suffer from deficits in adult neurogenesis. PMID: 24259590 These studies demonstrate that transactivation of the Gfap promoter is an early and sustained indicator of the disease process in the mouse. PMID: 23432455 These data suggest that all astroglia cells in the developing and adolescent mouse brain express GFAPdelta, regardless of their neurogenic capabilities. PMID: 23285135 The GFAP-stained intensity of the retinal area is increased in contralateral eyes and decreased in retinal ganglion cells of eyes with laser-induced ocular hypertension. PMID: 22583833 Postulate that glial cells with increased Gfap expression support the elongation of new neurites from retinal ganglion cells possibly by providing a scaffold for outgrowth. PMID: 23259929 GFAP expression is almost not affected by melatonin treatment in aged mice. PMID: 22200709 differential regulation of GFAP isoforms is not involved in the reorganization of the intermediate filament network in reactive gliosis or in neurogenesis in the mouse brain. PMID: 22912745 CD44-positive cells are APCs in the early postnatal cerebellum; surviving cells gradually express glial fibrillary acidic protein GFAP), a marker for mature astrocytes, indicating differentiation into mature astrocytes is the default for these cells. PMID: 21732075 GFAP-negative astrocytes are fully inflammation-competent, displaying phenotypic heterogeneity as is commonly observed in brain astrocytes. PMID: 22072312 In a mouse model of amyotrophic lateral sclerosis (ALS), GFAP is not necessary for the initiation of disease; instead, it plays some modulatory roles in the progression of ALS. PMID: 21453731 Treadmill exercise training decreased the expression of GFAP in the striatum of chronic Parkinsonian mice, which can partially explain the beneficial neuroprotective role of exercise in patients with parkinson disease. PMID: 21725169 The study shows opposing pattern of nestin and glial fibrillary acidic protein expression in mouse hippocampus occuring in early postnatal development, suggesting that it is important for neural differentiation and positioning in the hippocampus. PMID: 21368556 In the mouse there is a slight increase in the number of GFAP positive cells in the white matter after 3 days of severe cerebral contusion trauma. PMID: 20479526 Increased expression of GFAP in Muller cells of mer knockout mice occur at P20d in the peripheral retina and P4w in the central retina. GFAP expression in Muller cells appears to be a secondary response to the loss of retinal neurons. PMID: 20497693 One protein, GFAP (glial fibrillary acidic protein), was found to be elevated in the LINCL mice compared with normal controls in both isolated storage bodies and a lysosome-enriched subcellular fraction that contains storage material. PMID: 20370715 The results of this study suggested that GFAP is necessary for morphological retention and distribution of reactive astrocytes during prion disease, and that there is a GFAP-dependent function of glial filaments in reactive astrocytes. PMID: 19931516 Report demonstrated for the first time that GFAPdelta is specifically expressed in radial glia and SVZ neural progenitors during human brain development. PMID: 20040497 The exact expression of glial fibrillary acidic protein (GFAP) in trigeminal ganglion and dental pulp. PMID: 11838710 Human influenza viral infection in utero alters GFAP immunoreactivity in the developing brains of neonatal mice. PMID: 12140787

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.