KP-2031

HCAb-hIgG4-S228P-isotype

×
Please enable JavaScript in your browser to complete this form.
12301
Home » Antibodies » HCAb-hIgG4-S228P-isotype

Background of HCAb-hIgG4-S228P-isotype

Isotype controls are a type of primary antibodies that lack specificity to the target, but match the class and type of the primary antibody used in in vitro and in vivo studies. Isotype controls are often used to measure the level of non-specific background signal caused by binding non-specifically to Fc receptors on the cell surface, or other cellular molecules. Most antibodies consist of four components: two heavy chains and two light chains. This complexity makes their engineering challenging and recombinant expression difficult. Interestingly, camelids and sharks produce antibodies that are only composed of heavy chains (heavy chain antibodies, hcAbs). Although the hcAbs of camelids and sharks differ somewhat in structure, their single N-terminal domain (VHH and VNAR, respectively) contain the ability to bind an antigen without domain pairing using three complementarity-determining regions (CDRs). These N-terminal domains have been named single domain antibodies (sdAbs) or nanobodies and have become promising tools for life scientists, protein engineers and synthetic biologists alike.

Specifications

Catalog NumberKP-2031
Antibody NameHCAb-hIgG4-S228P-isotype
IsotypeHuman-IgG4-S228P-FC
TargetHEL
Species ReactivityChicken
Host Cell LineEXPI-CHO
Purification MethodAffinity purified
Concentration>2mg/mL
Formulation20mM sodium citrate,150mM NaCl, pH5.5
Purity>95% by SDS-PAGE and SEC-SEC-HPLC
ValidationSDS-PAGE | SEC-HPLC | ELISA
Endotoxin Level<0.5 EU/mg as determined by the LAL method
Sterility0.2μm filtered
StorageStable for twelve months from date of receipt when stored at -20°C to -80°C; Stored at 2-8°C for one month without detectable loss of activity.

Characterization

Application

References

  1. Vidarsson, G., Dekkers, G. & Rispens, T. IgG Subclasses and Allotypes: From Structure to Effector Functions. Front. Immunol. 5, (2014).
  2. Zhong, X. et al. Transient CHO expression platform for robust antibody production and its enhanced N-glycan sialylation on therapeutic glycoproteins. Biotechnol. Prog. 35, e2724 (2019).
Please enable JavaScript in your browser to complete this form.