Name: | Recombinant full length rat GFAP |
HGNC Name: | GFAP |
RRID: | NA |
Format: | 1mg/mL in 6M Urea |
Applications: | Protein standard for ELISA, MSD, Luminex and Simoa assays, immunogen for antibody production |
Storage: | Stable at 4°C for several months. For longer term store at -20°C or lower |
Uniprot: | P47819 |
Recombinant Rat GFAP
Cat# Prot-r-GFAP-rat
$300.00 – $2,000.00
Glial Fibrillary Acidic Protein (GFAP) is a major protein of the nervous system and is localized in astrocytes, stem cells, Bergmann glia and non-myelinating Schwann cells. It may also be found in retinal Mueller cells in pathological states, and the levels of the protein generally increase in damage and disease states (1-3). GFAP assembles to form 10nm or intermediate filaments in the cytoplasm, and these filaments appear to have an important structural role in the cell. Recent work suggests that measurement of the levels of GFAP in blood and CSF gives information about CNS damage and disease states (4).
This product is identical to the rat GFAP isotype I sequence in GenBank entry NP_058705.2. It can be used as a standard in ELISA and other antibody based assays on rodent animal damage and disease models. The human GFAP protein is a little different in amino acid sequence from the rat protein, so a recombinant form of the human protein is also available from EnCor, Prot-r-GFAP, for use with studies of human damage and disease states. The product data and MSDS information can be downloaded from the “Data Sheets” tab below.
Human GFAP sequence was based on that was NP_058705.2 which was inserted into the eukaryotic expression vector pET29a(+) which adds an C-terminal His tag and some other sequence, underlined below. This sequence includes an S-tag affinity peptide (red) and an enterokinase cleavage site (green).
MKE TAAAKFERQH MDSPDLG TLVPRGSMAD IGSEFMERRR ITSARRSYAS SETMVRGHGP 60
TRHLGTIPRL SLSRMTPPLP ARVDFSLAGA LNAGFKETRA SERAEMMELN DRFASYIEKV 120
RFLEQQNKAL AAELNQLRAK EPTKLADVYQ AELRELRLRL DQLTTNSARL EVERDNLTQD 180
LGTLRQKLQD ETNLRLEAEN NLAVYRQEAD EATLARVDLE RKVESLEEEI QFLRKIHEEE 240
VRELQEQLAQ QQVHVEMDVA KPDLTAALRE IRTQYEAVAT SNMQETEEWY RSKFADLTDV 300
ASRNAELLRQ AKHEANDYRR QLQALTCDLE SLRGTNESLE RQMREQEERH ARESASYQEA 360
LARLEEEGQS LKEEMARHLQ EYQDLLNVKL ALDIEIATYR KLLEGEENRI TIPVQTFSNL 420
QIRETSLDTK SVSEGHLKRN IVVKTVEMRD GEVIKESKQE HKDVMVDKLA AALEHHHHHH 480
Number of amino acids: 480
Molecular weight: 55497.31
Theoretical pI: 5.51
Amino acid composition:
Ala (A) 47 9.8%
Arg (R) 48 10.0%
Asn (N) 17 3.5%
Asp (D) 24 5.0%
Cys (C) 1 0.2%
Gln (Q) 30 6.2%
Glu (E) 65 13.5%
Gly (G) 14 2.9%
His (H) 16 3.3%
Ile (I) 14 2.9%
Leu (L) 58 12.1%
Lys (K) 23 4.8%
Met (M) 14 2.9%
Phe (F) 9 1.9%
Pro (P) 10 2.1%
Ser (S) 27 5.6%
Thr (T) 28 5.8%
Trp (W) 1 0.2%
Tyr (Y) 10 2.1%
Val (V) 24 5.0%
Total number of negatively charged residues (Asp + Glu): 89
Total number of positively charged residues (Arg + Lys): 71
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 20400
Abs 0.1% (=1 g/l) 0.368, assuming all pairs of Cys residues form cystines
Ext. coefficient 20400
Abs 0.1% (=1 g/l) 0.368, assuming all Cys residues are reduced
1. Bignami A, Eng LF, Dahl D, Uyeda CT. Localization of the glial fibrillary acidic protein in astrocytes by immunofluorescence. Brain Res. 43:429-35 (1972).
2. Brenner M, et al. Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease. Nat Genet 27:117-20 (2001).
3. Silver J. Miller JH. Regeneration beyond the glial scar. Nat. Rev. Neurosci. 5:146-56 (2004).
4. Schiff L1, Hadker N, Weiser S, Rausch C. A literature review of the feasibility of glial fibrillary acidic protein as a biomarker for stroke and traumatic brain injury. Mol. Diagn. Ther. 16:79-92 (2012).
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Contact info
EnCor Biotechnology Inc.
4949 SW 41st Boulevard, Ste 40
Gainesville
Florida 32608 USA
Phone: (352) 372 7022
Fax: (352) 372 7066
E-mail: admin@encorbio.com