Recombinant Rana japonica Sialic acid-binding lectin CSB-EP321644RJL
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Sialic acid-binding lectin; EC 3.1.27.-
Species: (Organism)
Rana japonica (Japanese reddish frog)
Gene Names:
N/A
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
QNWAKFQEKHIPNTSNINCNTIMDKSIYIVGGQCKERNTFIISSATTVKAICSGASTNRNVLSTTRFQLNTCIRSATAPRPCPYNSRTETNVICVKCENRLPVHFAGIGRC
Expression Region:
1-111aa
Subcellular Location:
Secreted
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
16.3 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:
Others
Function:
The S-lectins in frog eggs may be involved in the fertilization and development of the frog embryo. This lectin preferentially agglutinate a large variety of tumor cells, but it does not agglutinate non-transformed cells and erythrocytes.
Involvement in disease:
Relevance:
The S-lectins in frog eggs may be involved in the fertilization and development of the frog bryo. This lectin preferentially agglutinate a large variety of tumor cells, but it does not agglutinate non-transformed cells and erythrocytes.
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:
Pancreatic ribonuclease family
Reference:
Amino acid sequence of a lectin from Japanese frog (Rana japonica) eggs.Kamiya Y., Oyama F., Oyama R., Sakakibara F., Nitta K., Kawauchi H., Takayanagi Y., Titani K.J. Biochem. 108:139-143(1990)
