Recombinant Rat Glial Fibrillary Acidic Protein (GFAP) Protein (His)

Name: Recombinant Rat Glial Fibrillary Acidic Protein (GFAP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06933P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Rat Glial Fibrillary Acidic Protein (GFAP) 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.
Uniprotkb	P47819
Target Symbol	GFAP
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MERRRITSARRSYASSETMVRGHGPTRHLGTIPRLSLSRMTPPLPARVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTTNSARLEVERDNLTQDLGTLRQKLQDETNLRLEAENNLAVYRQEADEATLARVDLERKVESLEEEIQFLRKIHEEEVRELQEQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDVASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM
Expression Range	1-430aa
Protein Length	Full Length
Mol. Weight	55.9 kDa
Research Area	Neuroscience
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: rno:24387 STRING: 10116.ENSRNOP00000032389 UniGene: PMID: 29852171 The present study found that social isolation during adolescence resulted in abnormal locomotor, emotional and cognitive behaviors and increased the expression of GFAP, ANXA2 and VIM in PFC of adult rats PMID: 28705472 GFAP-positive structures were present and exhibited a tendency to become linear on both sides, with an increased density on the left. NFAP-positive expression was present in the left treated limb with a disorganized pattern PMID: 28652433 We found that GFAP exhibited enhanced stability upon the addition of two equivalents of each ligands with ceftriaxone imparting a more spontaneous interactions and a more ordered complex system than phenytoin PMID: 27133445 reduction of GFAP+ cell density was in agreement with a lower expression of GFAP protein PMID: 27579183 Astrocyte expression of GLAST/GFAP was reduced via JAK1/JAK2/STAT3 signaling pathway after exposure to sevoflurane. PMID: 27003918 Upon ependymal stem cells differentiation, Cx50 expression favors glial cell fate, since higher expression levels, endogenous or by over-expression of Cx50, augmented the expression of the astrocyte marker GFAP and impaired the neuronal marker Tuj1. PMID: 26561800 It is likely that a plastic change in GFAP expression in astrocytes selectively occurs around Oxytocin (OXT) neurons at proestrus and facilitates OXT release. PMID: 26994384 investigated temporal profile of astrocytic and neuronal injury markers after TBI; different mechanisms underlie clearance of UCH-L1 and GFAP in CSF and serum PMID: 25763798 Its antibody is able to protect cells from oxidative stress, which is due to changed protein expressions of the actin cytoskeleton. PMID: 25837926 GFAP release in hippocampus is significantly increased in a model of traumatic brain injury. PMID: 25898931 Hippocampal glucose uptake defects correlate with NeuN immunoreactivity in the latent phase and GFAP immunoreactivity in the chronic phase. PMID: 25798055 paracrine factors inhibit p38 MAPK and JNK, and most likely by regulating their downstream targets, p53 and STAT1, to promote astrocyte survival associated with GFAP downregulation after ischemic stroke in vitro PMID: 25752945 The down-regulation of histone deacetylase SIRT1 abrogating the effect of cocoa on glial fibrillary acidic protein up-regulation and on Lys310-RelA/p65 acetylation by silencing or blockage was clearly demonstrated herein in vivo and in vitro. PMID: 25448608 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 increased in nucleus ambiguous after recurrent or superior laryngeal nerve injury PMID: 25181319 Diametric expression of GFAP and a different morphological pattern of caspase-3 labelling, although no changes in the cell number, were observed in the neurons of young and old animals. PMID: 25182537 Progesterone promotes neuroprotection following traumatic brain injury by inhibiting the expression of Nogo-A and GFAP, and increasing GAP-43 expression. PMID: 24567055 GFAP expression study also showed that cortical layer I usually contained multiple large astrocytes with branching processes, as well as numerous smaller processes with high intensity of expression. PMID: 25282817 GFAP repression is mediated through direct binding of p-PPARgamma (S112) to its promoter region. PMID: 24481447 GFAP is an important marker in determining the severity of traumatic brain injury. PMID: 24379073 To clarify whether GFAP-positive neoplastic astrocytes exist in rat spontaneous oligodendrogliomas and mixed gliomas or not, immunohistochemical examination was performed on spontaneous oligodendrogliomas (26 cases) and mixed gliomas. PMID: 23076037 Findings indicate the reciprocal relationships between GFAP expression and astrocyte neurotrophic activity by linking the ERalpha to ERbeta ratio to GFAP expression. PMID: 23515288 TMJ inflammation induced significant upregulation of GFAP (an astroglial marker) in the trigeminal subnucleus caudalis. PMID: 23110394 Western blot analysis showed that the chronic stress downregulated GFAP but upregulated NDRG2 protein PMID: 22610521 In the hippocampus, thalamus, and piriform cortex both vascular laminin and astrocytic GFAP expression are upregulated following kainic acid injection. PMID: 22475395 Increases in c-fos and GFAP were triggered by the combined stress of non-thermal irradiation and the toxic effect of picrotoxin on cerebral tissues. PMID: 21524663 There was a reduction in GFAP levels in the hippocampus of non-trained diabetic animals, which was not found in trained diabetic group. PMID: 21892662 Zuogui Pill may have protective effects on the optic nerve and retina ganglion cells after contusion by promoting nestin and GFAP expressions in Muller cells of the retina. PMID: 21906524 Activation of a pro-survival IL-6/JAK2/STAT3 cascade contributes to cholera toxin-induced GFAP expression. PMID: 21470923 Cesarean section might increase GFAP expression in the hippocampus and frontal cortex, and trigger neuronal apoptosis of hippocampus region. PMID: 21211284 GFAP-positive temporomandibular joint disc cells were characterized by broader processes and existed exclusively in the deeper area. PMID: 21679183 GFAP expression was down-regulated while GAP-43 expression upregulated in the retinal ganglial cells after peripheral nerve transplantation. PMID: 20423852 Region-specific alterations in the gene expression of GFAP, VEGF, and FGF-2 and their receptors in the aged brain correspond to changes in astrocytic reactivity, supporting astrocytic heterogeneity and demonstrating a differential aging effect. PMID: 21385309 GFAP content was diminished after a long-term administration of progesterone in hippocampus. PMID: 21683086 There is a differential expression pattern of GFAP in the rat brain during pregnancy and the beginning of lactation that is associated with changes in brain function during these reproductive stages. PMID: 20732387 Data show that astrocyte structural proteins GFAP and vimentin are induced by chronic leptin administration, suggesting astrocytes participating in leptin modulated synaptic inputs. PMID: 21343257 Butylphthalide may protect the neuron-vascular unit of the hippocampus of Alzheimer model rats by inhibiting the expression of GFAP and increasing the expression of VEGF. PMID: 20197608 Pax3 negatively regulates GFAP expression during astrocyte differentiation in vitro PMID: 21371476 these results indicate that intracellular cAMP levels regulate the expression of NPP1 in rat C6 glioma cells by a signalling pathway that is different from the GFAP signal transduction pathway PMID: 21168404 hyperbaric oxygenation treatment for cerebral infarction, can increase the expression of Map-2 and decrease the expression of GFAP. PMID: 19141977 Amniotic fluid-GFAP levels appear to correlate with spinal cord injury as gestation proceeds in fetal rats with myelomeningocele. PMID: 21284970 Retinal injury induces an upregulation of a complement of four intermediate filament proteins, including synemin and nestin, in Muller cells. PMID: 21139996 Chondroitinase ABC can reduce the expression of GFAP after spinal cord injury. PMID: 21046809 retinoic acid and cytokines have a synergistic effect on the regulation of glial fibrillary acidic protein expression PMID: 20876578 There was no significant increase in GFAP immunoreactivity in the white matter in a weight drop model of mild cerebral contusion injury in the rat. PMID: 20479526 Alcohol could repress the expression of GFAP and S100 of astrocytes. PMID: 16986516 S100 protein and glial fibrillary acidic protein expression increased significantly in the hippocampal astrocytes of rats with Alzheimer disease, and were inhibited by butylphthalide. PMID: 19726345 Brain concussion induced the expression of GFAP. PMID: 16850587 expression of 25-kDa synaptosomal-associated protein and glial fibrillary acidic protein, were significantly enhanced in the cerebellum of rats with treadmill training after cerebral infarct PMID: 19661770

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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.

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