CAS 9007-83-4 γ-Globulins from rabbit - Analytical Products / Alfa Chemistry

CAT	AP9007834-C
CAS	9007-83-4
MDL Number	MFCD00165672
EC Number	232-706-1

Description	≥99% (agarose gel electrophoresis)
Solubility	0.9% NaCl: soluble 50 mg/mL; 0.9% NaCl: soluble 50 mg/mL
Assay	≥99% (agarose gel electrophoresis)
Impurity Content	≤5% NaCl
Size	1G
Storage Conditions	−20°C

"Protein A" From Staphylococcus Aureus. 3. Reaction With Rabbit Gamma-Globulin

A Forsgren, J Sjöquist

J Immunol. 1967 Jul;99(1):19-24.

PMID: 4166022

[Penetration of Gamma-Globulins From Mother to Fetus in the Rabbit (Liuminescent-Serologic Study)]

Iu N Zubzhitskiĭ, Z P Zhemkova

Tsitologiia. 1970 Feb;12(2):256-61.

PMID: 4194875

Interference of Non-Specific Gamma Globulins With Passive in Vitro Anaphylactic Sensitization of Isolated Guinea-Pig Intestine

R BINAGHI, P LIACOPOULOS, B N HALPERN, M LIACOPOULOS-BRIOT

Immunology. 1962 Mar;5(2):204-10.

PMID: 13869226

Recovery of Antibody Activity From Inactive Hybrids of H and L Chains

O A Roholt, G Radzimski, D Pressman

J Exp Med. 1967 Jan 1;125(1):191-7.

PMID: 4163359

The Isolation of Gamma-Globulins From Rat, Guinea Pig, and Rabbit Plasma

J GOLDSTEIN, J W ANDERSON

J Biol Chem. 1957 Feb;224(2):775-81.

PMID: 13405906

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Case Study

Rabbit Gamma-Globulins for Enhanced Surface Functionalization in Click Chemistry Applications

Vrettou, Fotini, et al. Surfaces and Interfaces 36 (2023): 102500.

Rabbit gamma-globulins (IgG) play a crucial role in improving surface functionalization efficiency, particularly in bioorthogonal click chemistry. A recent study evaluated the impact of IgG coating on silicon surfaces modified via two distinct protocols: EPRmed and APTES in toluene. The goal was to assess the efficiency of sulfo-NHS-DBCO conjugation and subsequent azide-fluorophore labeling.
Silicon surfaces were pre-modified with either EPRmed or APTES, followed by IgG immobilization to maximize surface coverage. Subsequent conjugation with sulfo-NHS-DBCO and reaction with 5-FAM-azide allowed differentiation between specific and non-specific fluorophore binding. Fluorescence microscopy revealed a threefold increase in fluorescence signal when EPRmed surfaces were coated with IgG, compared to uncoated surfaces. Extending the reaction time to 24 hours further enhanced fluorescence intensity by 4.5 times. However, APTES-modified surfaces showed minimal fluorescence enhancement with IgG coating, suggesting lower efficiency in facilitating bioorthogonal reactions.
The study also highlighted the influence of surface modification thickness on fluorescence uniformity. The ~1 µm EPRmed layer led to localized protein accumulation, causing heterogeneous fluorescence intensity, whereas the ~1 nm APTES layer exhibited more uniform binding.
These findings establish rabbit gamma-globulins as valuable agents for improving surface biofunctionalization in click chemistry. Their role in enhancing coupling efficiency makes them essential for biosensing, diagnostics, and biomolecular immobilization applications.

Rabbit γ-Globulins for Molecularly Imprinted Polymers: Investigating Binding Site Distribution and Cooperativity

Testa, Valentina, et al. ACS Applied Polymer Materials (2025).

Rabbit γ-globulins serve as a critical template in the synthesis of nanosized molecularly imprinted polymers (nanoMIPs), influencing binding site distribution and ligand interaction mechanisms. Recent studies have explored the binding behavior of nanoMIPs designed for rabbit γ-globulins, comparing them to those imprinted with smaller molecules like ciprofloxacin.
NanoMIPs are typically assumed to follow a heterogeneous binding affinity model, as described by the Langmuir-Freundlich isotherm. However, experimental data indicate that nanoMIPs targeting ciprofloxacin exhibit positive cooperativity, suggesting that binding site proximity may enhance ligand recognition. In contrast, nanoMIPs synthesized using rabbit γ-globulins as templates do not demonstrate cooperative binding. This discrepancy is attributed to the macromolecular size of γ-globulins, which sterically hinder close binding site formation during polymer cross-linking.
An increase in cross-linking density (from 1% to 20%) resulted in a reduced binding site density but a significant rise in apparent equilibrium binding constants, confirming that steric effects influence site distribution. Scatchard plots of γ-globulin nanoMIPs showed linearity across all binding data, contrasting with the convex plots observed for ciprofloxacin nanoMIPs. This further supports the hypothesis that binding cooperativity in nanoMIPs is strongly dependent on the spatial arrangement of recognition sites.
These findings highlight the importance of template selection in nanoMIP design, positioning rabbit γ-globulins as a valuable tool for studying steric effects in molecular imprinting and optimizing biomacromolecule recognition in diagnostic and biosensing applications.