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Glial fibrillary acidic protein (GFAP)

 GFAP_MOUSE              Reviewed;         430 AA.
P03995; A1E2H7; A2AH87; B2RTI7; Q09J71; Q3USS4; Q496R4; Q496S3;
Q7TQ30; Q80VX6; Q925K2; Q925K3;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 4.
25-OCT-2017, entry version 160.
RecName: Full=Glial fibrillary acidic protein;
Short=GFAP;
Name=Gfap;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2994002; DOI=10.1093/nar/13.15.5527;
Balcarek J.M., Cowan N.J.;
"Structure of the mouse glial fibrillary acidic protein gene:
implications for the evolution of the intermediate filament multigene
family.";
Nucleic Acids Res. 13:5527-5543(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
STRAIN=129/Sv;
Sheng J., Wu X., Lin F., Yang X., Deng J.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
TISSUE=Embryo;
PubMed=7983160;
Ralton J.E., Lu X., Hutcheson A.M., Quinlan R.A.;
"Identification of two N-terminal non-alpha-helical domain motifs
important in the assembly of glial fibrillary acidic protein.";
J. Cell Sci. 107:1935-1948(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1).
PubMed=6585825; DOI=10.1073/pnas.81.9.2743;
Lewis S.A., Balcarek J.M., Krek V., Shelanski M., Cowan N.J.;
"Sequence of a cDNA clone encoding mouse glial fibrillary acidic
protein: structural conservation of intermediate filaments.";
Proc. Natl. Acad. Sci. U.S.A. 81:2743-2746(1984).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1).
PubMed=3866511; DOI=10.1111/j.1749-6632.1985.tb50437.x;
Cowan N.J., Lewis S.A., Balcarek J.M., Krek V., Shelanski M.L.;
"Structural implications of a cDNA clone encoding mouse glial
fibrillary acidic protein.";
Ann. N. Y. Acad. Sci. 455:575-582(1985).
[9]
SEQUENCE REVISION TO N-TERMINUS.
PubMed=2163003; DOI=10.1016/0169-328X(90)90078-R;
Brenner M., Lampel K., Nakatani Y., Mill J., Banner C., Mearow K.,
Dohadwala M., Lipsky R., Freese E.;
"Characterization of human cDNA and genomic clones for glial
fibrillary acidic protein.";
Brain Res. Mol. Brain Res. 7:277-286(1990).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-430 (ISOFORM 1).
STRAIN=ISS;
PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
"High-throughput sequence identification of gene coding variants
within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 92-275 (ISOFORMS 1/2).
STRAIN=C57BL/6J;
Huysentruyt L.C., Banerjee D., Seyfried T.N.;
"Novel metastatic mouse tumor cells express multiple properties of
macrophages.";
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[12]
PROTEIN SEQUENCE OF 47-63; 139-149; 187-198; 210-233; 285-297 AND
374-387, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (MAR-2007) to UniProtKB.
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 169-237 (ISOFORMS 1/2).
STRAIN=SJL/JHanHsd; TISSUE=Brain;
Ulrich R., Alldinger S., Baumgaertner W.;
"Progressive demyelination despite a temporary increased number of NG-
2 positive putative oligodendroglial progenitor cells in Theiler`s
murine encephalomyelitis.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[14]
PROTEIN SEQUENCE OF 354-364, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-430 (ISOFORM 2).
TISSUE=Blood;
PubMed=12837269; DOI=10.1016/S0888-7543(03)00106-X;
Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L.;
"Genetic polymorphism and sequence evolution of an alternatively
spliced exon of the glial fibrillary acidic protein gene, GFAP.";
Genomics 82:185-193(2003).
[16]
TISSUE SPECIFICITY.
PubMed=12058025; DOI=10.1074/jbc.M112121200;
Nielsen A.L., Holm I.E., Johansen M., Bonven B., Jorgensen P.,
Jorgensen A.L.;
"A new splice variant of glial fibrillary acidic protein GFAPepsilon,
interacts with the presenilin proteins.";
J. Biol. Chem. 277:29983-29991(2002).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[18]
INTERACTION WITH SYNM.
PubMed=17356066; DOI=10.1242/jcs.03423;
Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M.,
Skalli O.;
"Synemin is expressed in reactive astrocytes in neurotrauma and
interacts differentially with vimentin and GFAP intermediate filament
networks.";
J. Cell Sci. 120:1267-1277(2007).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-11 AND ARG-20, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- 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.
-!- SUBUNIT: Interacts with SYNM. {ECO:0000269|PubMed:17356066}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated
with intermediate filaments. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=GFAP alpha;
IsoId=P03995-1; Sequence=Displayed;
Name=2; Synonyms=GFAP epsilon;
IsoId=P03995-2; Sequence=VSP_017053;
-!- TISSUE SPECIFICITY: Brain; isoform 2 expressed at 20-fold lower
level than isoform 1. {ECO:0000269|PubMed:12058025}.
-!- PTM: Phosphorylated by PKN1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- SEQUENCE CAUTION:
Sequence=CAA26571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X02801; CAA26571.1; ALT_INIT; Genomic_DNA.
EMBL; AK140151; BAE24257.1; -; mRNA.
EMBL; AL731670; CAM25115.1; -; Genomic_DNA.
EMBL; AY279974; AAP33501.1; -; Genomic_DNA.
EMBL; X78141; CAA55020.1; -; Genomic_DNA.
EMBL; BC100728; AAI00729.1; -; mRNA.
EMBL; BC100737; AAI00738.1; -; mRNA.
EMBL; BC101968; AAI01969.1; -; mRNA.
EMBL; BC103571; AAI03572.1; -; mRNA.
EMBL; BC139357; AAI39358.1; -; mRNA.
EMBL; BC139358; AAI39359.1; -; mRNA.
EMBL; K01347; AAA37678.1; -; mRNA.
EMBL; M25937; AAA37679.1; -; mRNA.
EMBL; AF332061; AAK56090.1; -; mRNA.
EMBL; AF332062; AAK56091.1; -; mRNA.
EMBL; EF101554; ABK96803.1; -; mRNA.
EMBL; DQ887822; ABI54133.1; -; mRNA.
EMBL; AY142200; AAN87913.1; -; Genomic_DNA.
CCDS; CCDS25507.1; -. [P03995-1]
CCDS; CCDS48950.1; -. [P03995-2]
PIR; B60052; VEMSGF.
RefSeq; NP_001124492.1; NM_001131020.1. [P03995-2]
RefSeq; NP_034407.2; NM_010277.3. [P03995-1]
UniGene; Mm.1239; -.
ProteinModelPortal; P03995; -.
SMR; P03995; -.
BioGrid; 199899; 5.
DIP; DIP-1084N; -.
IntAct; P03995; 5.
MINT; MINT-4095997; -.
STRING; 10090.ENSMUSP00000064691; -.
iPTMnet; P03995; -.
PhosphoSitePlus; P03995; -.
UCD-2DPAGE; P03995; -.
MaxQB; P03995; -.
PaxDb; P03995; -.
PeptideAtlas; P03995; -.
PRIDE; P03995; -.
Ensembl; ENSMUST00000067444; ENSMUSP00000064691; ENSMUSG00000020932. [P03995-1]
Ensembl; ENSMUST00000077902; ENSMUSP00000077061; ENSMUSG00000020932. [P03995-2]
GeneID; 14580; -.
KEGG; mmu:14580; -.
UCSC; uc007lsw.2; mouse. [P03995-1]
UCSC; uc007lsx.2; mouse. [P03995-2]
CTD; 2670; -.
MGI; MGI:95697; Gfap.
eggNOG; ENOG410IJXF; Eukaryota.
eggNOG; ENOG410Y9QE; LUCA.
GeneTree; ENSGT00830000128228; -.
HOVERGEN; HBG013015; -.
InParanoid; P03995; -.
KO; K05640; -.
OMA; MQETEEW; -.
OrthoDB; EOG091G12MK; -.
PhylomeDB; P03995; -.
TreeFam; TF330122; -.
PRO; PR:P03995; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020932; -.
CleanEx; MM_GFAP; -.
Genevisible; P03995; MM.
GO; GO:0097450; C:astrocyte end-foot; IDA:MGI.
GO; GO:0097449; C:astrocyte projection; IDA:MGI.
GO; GO:0044297; C:cell body; IDA:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IEA:Ensembl.
GO; GO:0097386; C:glial cell projection; IDA:MGI.
GO; GO:0005882; C:intermediate filament; IDA:MGI.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
GO; GO:0005622; C:intracellular; IDA:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; IMP:MGI.
GO; GO:0014002; P:astrocyte development; IGI:MGI.
GO; GO:0060020; P:Bergmann glial cell differentiation; IMP:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
GO; GO:0045103; P:intermediate filament-based process; IMP:MGI.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:MGI.
GO; GO:0031102; P:neuron projection regeneration; IMP:MGI.
GO; GO:0010625; P:positive regulation of Schwann cell proliferation; IMP:MGI.
GO; GO:1904714; P:regulation of chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0051580; P:regulation of neurotransmitter uptake; IMP:MGI.
GO; GO:0009611; P:response to wounding; IEA:Ensembl.
InterPro; IPR027701; GFAP.
InterPro; IPR001664; IF.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR018039; Intermediate_filament_CS.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF41; PTHR23239:SF41; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Alternative splicing; Citrullination; Coiled coil; Complete proteome;
Cytoplasm; Direct protein sequencing; Intermediate filament;
Methylation; Phosphoprotein; Reference proteome.
CHAIN 1 430 Glial fibrillary acidic protein.
/FTId=PRO_0000063806.
DOMAIN 66 374 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 69 Head.
REGION 70 101 Coil 1A.
REGION 102 112 Linker 1.
REGION 113 211 Coil 1B.
REGION 212 227 Linker 12.
REGION 228 249 Coil 2A.
REGION 250 253 Linker 2.
REGION 254 374 Coil 2B.
REGION 375 430 Tail.
MOD_RES 7 7 Phosphothreonine; by AURKB and ROCK1.
{ECO:0000250|UniProtKB:P14136}.
MOD_RES 11 11 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 12 12 Phosphoserine; by AURKB and ROCK1.
{ECO:0000250|UniProtKB:P14136}.
MOD_RES 20 20 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 33 33 Citrulline. {ECO:0000250}.
MOD_RES 35 35 Phosphoserine; by AURKB and ROCK1.
{ECO:0000250|UniProtKB:P14136}.
MOD_RES 40 40 Phosphothreonine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000250|UniProtKB:P47819}.
MOD_RES 107 107 Phosphothreonine.
{ECO:0000250|UniProtKB:P47819}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000250|UniProtKB:P47819}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000250|UniProtKB:P47819}.
MOD_RES 267 267 Citrulline. {ECO:0000250}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000250|UniProtKB:P47819}.
MOD_RES 380 380 Phosphothreonine.
{ECO:0000250|UniProtKB:P47819}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000250|UniProtKB:P47819}.
MOD_RES 403 403 Citrulline. {ECO:0000250}.
MOD_RES 413 413 Citrulline. {ECO:0000250}.
VAR_SEQ 388 430 ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKDSKQEHKDV
VM -> GGKSTKEGEGQKVTRPLKRLTIQVVPIQAHQIENG
ALPALP (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017053.
CONFLICT 141 141 F -> L (in Ref. 5; AAP33501 and 10;
AAK56091). {ECO:0000305}.
CONFLICT 174 174 D -> H (in Ref. 1; CAA26571, 7; AAA37678,
8; AAA37679 and 13; ABI54133).
{ECO:0000305}.
CONFLICT 180 180 R -> S (in Ref. 2; BAE24257).
{ECO:0000305}.
CONFLICT 207 207 E -> D (in Ref. 1; CAA26571, 7; AAA37678
and 8; AAA37679). {ECO:0000305}.
CONFLICT 347 347 Q -> H (in Ref. 1; CAA26571).
{ECO:0000305}.
SEQUENCE 430 AA; 49900 MW; C0FB500AE1588377 CRC64;
MERRRITSAR RSYASETVVR GLGPSRQLGT MPRFSLSRMT PPLPARVDFS LAGALNAGFK
ETRASERAEM MELNDRFASY IEKVRFLEQQ NKALAAELNQ LRAKEPTKLA DVYQAELREL
RLRLDQLTAN SARLEVERDN FAQDLGTLRQ KLQDETNLRL EAENNLAAYR QEADEATLAR
VDLERKVESL EEEIQFLRKI YEEEVRELRE QLAQQQVHVE MDVAKPDLTA ALREIRTQYE
AVATSNMQET EEWYRSKFAD LTDAASRNAE LLRQAKHEAN DYRRQLQALT CDLESLRGTN
ESLERQMREQ EERHARESAS YQEALARLEE EGQSLKEEMA RHLQEYQDLL NVKLALDIEI
ATYRKLLEGE ENRITIPVQT FSNLQIRETS LDTKSVSEGH LKRNIVVKTV EMRDGEVIKD
SKQEHKDVVM


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MC-044 Glial Fibrillary Acidic Protein (GFAP) 200 uL


 

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