Recombinant Serratia marcescens Hemophore HasA(hasA) CSB-EP684482SYN
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Heme acquisition system protein A
Species: (Organism)
Serratia marcescens
Gene Names:
hasA
Tag info:
N-terminal 6xHis-SUMO-tagged
Target Protein AA Sequence:
MAFSVNYDSSFGGYSIHDYLGQWASTFGDVNHTNGNVTDANSGGFYGGSLSGSQYAISSTANQVTAFVAGGNLTYTLFNEPAHTLYGQLDSLSFGDGLSGGDTSPYSIQVPDVSFGGLNLSSLQAQGHDGVVHQVVYGLMSGDTGALETALNGILDDYGLSVNSTFDQVAAATAVGVQHADSPELLAA
Expression Region:
1-188aa
Subcellular Location:
Secreted
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
35.3 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:
Microbiology
Function:
Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.
Involvement in disease:
Relevance:
Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.
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:
Reference:
"Iron acquisition from heme and hemoglobin by a Serratia marcescens Extracellular domain protein."Letoffe S., Ghigo J.-M., Wandersman C.Proc. Natl. Acad. Sci. U.S.A. 91:9876-9880(1994)
