Analytical Data
-
Gene name
tbpA
- Application
-
Alternative Names
tbpA；PALB；Transthyretin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P02766
-
Expression Region
21-147aa
-
AA Sequence
GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS GPRRYTIAAL LSPYSYSTTA VVTNPKE
-
Molecular Weight
15.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The research on the recombinant protein tbpA focuses on the molecular mechanisms of bacterial iron acquisition, particularly in pathogenic strains of Neisseria species, such as Neisseria meningitidis and Neisseria gonorrhoeae. TbpA, or transferrin-binding protein A, is a crucial component of the bacterial outer membrane that plays a significant role in the uptake of iron from human transferrin, an essential process for bacterial survival and virulence. Understanding tbpA's structure and function can provide insights into the host-pathogen interaction, as well as the mechanisms bacteria use to evade the host's immune response. The production of recombinant tbpA enables researchers to study its biochemical properties in detail and may facilitate the development of potential vaccines or therapeutic strategies against Neisseria infections. Moreover, the study of tbpA could contribute to a broader understanding of metal ion transport in various pathogenic bacteria, highlighting its potential as a target for novel antimicrobial therapies.
