| Name: | Recombinant full length human GFAP |
| HGNC Name: | GFAP |
| RRID: | NA |
| Format: | 1mg/mL in 6M Urea, 10mM phosphate pH=7.5 |
| 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: | P14136 |
0.5 and 1 µg of recombinant GFAP based on the human isotype I sequence was expressed in and purified from E. coli using standard methods and run out for SDS-PAGE in lanes on the left as indicated. The two rightmost lanes show 0.5 and 1 µg of BSA protein standard. Lane S shows protein standards of the indicated molecular weights, gel was stained with Coomassie brilliant blue protein stain.
Recombinant Human GFAP Protein
Cat# Prot-r-GFAP
$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 human GFAP isotype I sequence in GenBank entry NP_002046.1. It is widely used as a standard in ELISA and other antibody based assays. The human GFAP protein is a little different in amino acid sequence from that of the rat protein, so a recombinant form of the rat protein is also available from EnCor, Prot-r-GFAP-rat. The product data and MSDS information can be downloaded from the “Data Sheets” tab below.
Human GFAP sequence was based on that was NP_002046.1 which was inserted into the eukaryotic expression vector pET30a(+) which adds an N-terminal His tag and some other sequence, underlined below. This sequence includes a thrombin cleavage site (blue), an S-tag affinity peptide (red) and an enterokinase cleavage site (green).
MHHHHHHSSG LVPRGSGMKE TAAAKFERQH MDSPDLGTDD DDKAMADIGS EFMERRRITS 60
AARRSYVSSG EMMVGGLAPG RRLGPGTRLS LARMPPPLPT RVDFSLAGAL NAGFKETRAS 120
ERAEMMELND RFASYIEKVR FLEQQNKALA AELNQLRAKE PTKLADVYQA ELRELRLRLD 180
QLTANSARLE VERDNLAQDL ATVRQKLQDE TNLRLEAENN LAAYRQEADE ATLARLDLER 240
KIESLEEEIR FLRKIHEEEV RELQEQLARQ QVHVELDVAK PDLTAALKEI RTQYEAMASS 300
NMHEAEEWYR SKFADLTDAA ARNAELLRQA KHEANDYRRQ LQSLTCDLES LRGTNESLER 360
QMREQEERHV REAASYQEAL ARLEEEGQSL KDEMARHLQE YQDLLNVKLA LDIEIATYRK 420
LLEGEENRIT IPVQTFSNLQ IRETSLDTKS VSEGHLKRNI VVKTVEMRDG EVIKESKQEH 480
KDVM 484
Number of amino acids: 484
Molecular weight: 55588.41
Theoretical pI: 5.47
Amino acid composition:
Ala (A) 52 10.7%
Arg (R) 49 10.1%
Asn (N) 17 3.5%
Asp (D) 28 5.8%
Cys (C) 1 0.2%
Gln (Q) 27 5.6%
Glu (E) 63 13.0%
Gly (G) 18 3.7%
His (H) 15 3.1%
Ile (I) 14 2.9%
Leu (L) 58 12.0%
Lys (K) 24 5.0%
Met (M) 16 3.3%
Phe (F) 9 1.9%
Pro (P) 11 2.3%
Ser (S) 28 5.8%
Thr (T) 22 4.5%
Trp (W) 1 0.2%
Tyr (Y) 10 2.1%
Val (V) 21 4.3%
Total number of negatively charged residues (Asp + Glu): 91
Total number of positively charged residues (Arg + Lys): 73
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient
Abs 0.1% (=1 g/l) 0.367, assuming all pairs of Cys residues form cystines
Ext. coefficient
Abs 0.1% (=1 g/l) 0.367, 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).
