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Recombinant Human GFAP Protein, >95% (SDS-PAGE), high purity

  • Azide Free
  • Carrier Free
  • ≥95%(SDS-PAGE)
Features and benefits
  • Expression System: E. coli
  • Protein Tag: N-His
Item Number
rp156642
Grouped product items
SKUSizeAvailabilityPrice Qty
rp156642-10μg
10μg
In stock
$159.90
rp156642-100μg
100μg
In stock
$899.90
rp156642-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$4,999.90

Carrier Free, >95% (SDS-PAGE), E.coli, His Tag, 1-432 aa

Basic Description

Product NameRecombinant Human GFAP Protein, >95% (SDS-PAGE), high purity
SynonymsGlial Fibrillary Acidic Protein | ALXDRD | FLJ45472 | GFAP astrocytes | GFAP | wu:fb34h11 | cb345 | etID36982.3 | FLJ42474 | GFAP_HUMAN | gfapl | Intermediate filament protein | wu:fk42c12 | xx:af506734 | zgc:110485 | GFAP | Glial Fibrillary Acidic Protei
GradeAzide Free, Carrier Free
Product Description

Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.
Description:
GFAP (Glial fibrillary acidic protein) is a type III intermediate filament protein. It is the major component of astrocyte intermediate filament. Defects in GFAP are a cause of Alexander disease. Alexander disease is a rare disorder of the central nervous system. It is a progressive leukoencephalopathy whose hallmark is the widespread accumulation of Rosenthal fibers which are cytoplasmic inclusions in astrocytes. At the amino acid sequence level, human GFAP shares 91% and 90% identity with rat and mouse GFAP, respectively.

Specifications & PurityCarrier Free, Azide Free, ≥95%(SDS-PAGE)
Purity>95% (SDS-PAGE)
Expression SystemE. coli
Amino Acids1-432 aa
SequenceMGHHHHHHMERRRITSAARRSYVSSGEMMVGGLAPGRRLGPGTRLSLARMPPPLPTRVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVELDVAKPDLTAALKEIRTQYEAMAS
Protein TagN-His
Predicted molecular weight49.9 kDa
SDS-PAGE50.0 kDa, under reducing conditions.

Images

Recombinant Human GFAP Protein (rp156642) - SDS-PAGE
3 μg/lane of Recombinant Human GFAP Protein (rp156642) was resolved with SDS-PAGE under reducing (R) and visualized by Coomassie® Blue staining, showing a band at 50.0 kDa under reducing conditions.

Product Specifications

FormLyophilized
ReconstitutionWe recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 1.0 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilu
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStore at -20°C for 1 year, store at 2-8℃ for 1 month. Avoid freeze / thaw cycle.

Certificates

Certificate of Analysis(COA)

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3 results found

Lot NumberCertificate TypeDateItem
ZJ24F0303061Certificate of AnalysisMar 08, 2024 rp156642
ZJ24F0303060Certificate of AnalysisMar 08, 2024 rp156642
ZJ24R0200298Certificate of AnalysisFeb 29, 2024 rp156642

Related Documents

References

1. Duguid, J R JR, Bohmont, C W CW, Liu, N G NG and Tourtellotte, W W WW..  (1989)  Changes in brain gene expression shared by scrapie and Alzheimer disease..  Proceedings of the National Academy of Sciences of the United States of America,      [PMID:2780570]
2. Kosako, H H and 6 more authors..  (1997)  Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase..  The Journal of biological chemistry,    (18):   [PMID:9099667]
3. Matsuzawa, K K and 10 more authors..  (1997)  Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN..  Biochemical and biophysical research communications,    (29):   [PMID:9175763]
4. Isaacs, A A, Baker, M M, Wavrant-De Vrièze, F F and Hutton, M M..  (1998)  Determination of the gene structure of human GFAP and absence of coding region mutations associated with frontotemporal dementia with parkinsonism linked to chromosome 17..  Genomics,    (1):   [PMID:9693047]
5. Brenner, M M and 5 more authors..  (2001)  Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease..  Nature genetics,      [PMID:11138011]
6. Nielsen, Anders Lade AL and 5 more authors..  (2002)  A new splice variant of glial fibrillary acidic protein, GFAP epsilon, interacts with the presenilin proteins..  The Journal of biological chemistry,    (16):   [PMID:12058025]
7. Kawajiri, Aie A and 6 more authors..  (2003)  Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase..  Molecular biology of the cell,      [PMID:12686604]
8. Lee, Jung Mu and 8 more authors..  (2006)  A case of infantile Alexander disease accompanied by infantile spasms diagnosed by DNA analysis..  Journal of Korean medical science,      [PMID:17043438]
9. Hinttala, Reetta R and 5 more authors..  (2007)  Alexander disease with occipital predominance and a novel c.799G>C mutation in the GFAP gene..  Acta neuropathologica,      [PMID:17805552]
10. Ye Wu and 5 more authors..  (2008)  Clinical and genetic study in Chinese patients with Alexander disease..  Journal of child neurology,      [PMID:18079314]
11. Kaneko, Hiroyuki H and 10 more authors..  (2009)  Novel GFAP mutation in patient with adult-onset Alexander disease presenting with spastic ataxia..  Movement disorders : official journal of the Movement Disorder Society,    (15):   [PMID:19412928]
12. Namekawa, Michito M and 5 more authors..  (2010)  Adult-onset Alexander disease with typical "tadpole" brainstem atrophy and unusual bilateral basal ganglia involvement: a case report and review of the literature..  BMC neurology,    (1):   [PMID:20359319]
13. Jin, Zhicheng and 5 more authors..  (2013)  Identification and characterization of citrulline-modified brain proteins by combining HCD and CID fragmentation..  Proteomics,      [PMID:23828821]

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