Recombinant Human Glycophorin-A (GYPA),partial CSB-YP010074HU
Specifications
| 20ug / 100ug price = 20ug |
Alternative Name(s):
MN sialoglycoprotein;PAS-2Sialoglycoprotein alpha; CD235a
Species: (Organism)
Homo sapiens (Human)
Gene Names:
GYPA
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
LSTTEVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPE
Expression Region:
20-91aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Extracellular Domain
Pathway:
Mol. Weight:
9.9 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:
Cardiovascular
Function:
Involvement in disease:
Relevance:
Glycophorin A is the major intrinsic mbrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte mbrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma mbrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).
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:
Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane.Yajima A., Urano-Tashiro Y., Shimazu K., Takashima E., Takahashi Y., Konishi K.Microbiol. Immunol. 52:69-77(2008)
