Recombinant Human Mitochondrial import inner membrane translocase subunit Tim17-A(TIMM17A) CSB-EP023550HU
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Inner membrane preprotein translocase Tim17a
Species: (Organism)
Homo sapiens (Human)
Gene Names:
TIMM17A
Tag info:
N-terminal GST-tagged
Target Protein AA Sequence:
MEEYAREPCPWRIVDDCGGAFTMGTIGGGIFQAIKGFRNSPVGVNHRLRGSLTAIKTRAPQLGGSFAVWGGLFSMIDCSMVQVRGKEDPWNSITSGALTGAILAARNGPVAMVGSAAMGGILLALIEGAGILLTRFASAQFPNGPQFAEDPSQLPSTQLPSSPFGDYRQYQ
Expression Region:
1-171aa
Subcellular Location:
Mitochondrion inner membrane, Multi-pass membrane protein
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
45 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Signal Transduction
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Involvement in disease:
Relevance:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Tim17/Tim22/Tim23 family
Reference:
"The preprotein translocase of the inner mitochondrial membrane: evolutionary conservation of targeting and assembly of Tim17." Boemer U., Rassow J., Zufall N., Pfanner N., Meijer M., Maarse A.C. J. Mol. Biol. 262:389-395(1996)
