Antibodies, Proteins, Kits and Reagents for Life Science

Key features and details

Expression system: Wheat germ
Suitable for: SDS-PAGE, ELISA, WB

Product name

Recombinant Human FABP-1 protein
See all FABP-1 proteins and peptides
Expression system

Wheat germ
Accession

P00505
Protein length

Protein fragment
Animal free

No
Nature

Recombinant
- Species
  
  Human
- Sequence
  
  LNTPDLRKQWLQEVKGMADRIIGMRTQLVSNLKKEGSTHNWQHITDQIGM FCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVTK
- Predicted molecular weight
  
  37 kDa
- Amino acids
  
  331 to 430

Alternative names
- AATM_HUMAN
- AL022787
- Aspartate aminotransferase
- Aspartate aminotransferase 2
- Aspartate aminotransferase, mitochondrial
- Aspartate transaminase 2
- ASPATA
- EC 2.6.1.1
- FABP 1
- FABP pm
- FABP-1
- FABPpm
- Fatty acid binding protein
- Fatty acid-binding protein
- FLJ40994
- Glutamate oxaloacetate transaminase 2
- Glutamate oxaloacetate transaminase 2, mitochondrial
- Glutamate oxaloacetate transaminase, mitochondrial
- Glutamic oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)
- Got 2
- GOT2
- KAT4
- KATIV
- kynurenine aminotransferase 4
- Kynurenine aminotransferase IV
- kynurenine--oxoglutarate transaminase 4
- kynurenine--oxoglutarate transaminase IV
- mAspAT
- MGC102129
- MGC115763
- mitAAT
- mitochondrial
- Mitochondrial aspartate aminotransferase
- OTTMUSP00000017748
- Plasma membrane fatty acid binding protein
- Plasma membrane-associated fatty acid-binding protein
- Transaminase A
see all
Function

Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.
Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Cellular localization

Mitochondrion matrix. Cell membrane. Exposure to alcohol promotes translocation to the cell membrane.
Target information above from: UniProt accession P00505 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt

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