Recombinant Human Immunoglobulin J chain(JCHAIN) CSB-BP011337HU
Specifications
| 20ug / 100ug price = 20ug |
Alternative Name(s):
Joining chain of multimeric IgA and IgM
Species: (Organism)
Homo sapiens (Human)
Gene Names:
JCHAIN
Tag info:
N-terminal MBP-tagged and C-terminal 6xHis-tagged
Target Protein AA Sequence:
QEDERIVLVDNKCKCARITSRIIRSSEDPNEDIVERNIRIIVPLNNRENISDPTSPLRTRFVYHLSDLCKKCDPTEVELDNQIVTATQSNICDEDSATETCYTYDRNKCYTAVVPLVYGGETKMVETALTPDACYPD
Expression Region:
23-159aa
Subcellular Location:
Secreted
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
59.6 kDa
Purity:
Greater than 85% 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:
Immunology
Function:
Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component.
Involvement in disease:
Relevance:
Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component.
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:
"Primary structure of human J chain: alignment of peptides from chemical and enzymatic hydrolyses." Mole J.E., Bhown A.S., Bennett J.C. Biochemistry 16:3507-3513(1977)
