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Citations & References (4)
Invitrogen™
Recombinant Protein G - Sepharose™ 4B
Recombinant protein G is produced in a strain of E. coli which contains the gene for protein G from StreptococcusRead more
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| Catalog Number | Quantity |
|---|---|
| 101241 | 2 mL |
| 101242 | 5 mL |
| 101243 | 25 mL |
Catalog number 101241
Price (KRW)
436,000
온라인 행사
Ends: 31-Mar-2026
512,000Save 76,000 (15%)
Each
Quantity:
2 mL
Price (KRW)
436,000
온라인 행사
Ends: 31-Mar-2026
512,000Save 76,000 (15%)
Each
Recombinant protein G is produced in a strain of E. coli which contains the gene for protein G from Streptococcus sp. This product is prepared by covalently coupling highly purified rec-Protein G to Sepharose™ 4B. It is supplied as a 50% suspension containing 25 ml rec-Protein G-Sepharose™ 4B + 25 ml PBS (10 mM phosphate-buffered saline, pH 7.4, containing 0.19% Kathon CG/ICP).
Applications: Immunoglobulin affinity purification and Immunoprecipitation.
Recombinant protein G binds to the Fc region of many types of immunoglobulin G including:
• all four subclasses of human IgG
• mouse IgG
• rabbit IgG
• guinea pig IgG
• rat IgG
• goat IgG
• sheep IgG
• cow IgG
• horse IgG
Recombinant protein G does not bind to IgG from chicken or cat, or to human IgA, IgM, or serum albumin. It binds weakly to IgG from dog.
Applications: Immunoglobulin affinity purification and Immunoprecipitation.
Recombinant protein G binds to the Fc region of many types of immunoglobulin G including:
• all four subclasses of human IgG
• mouse IgG
• rabbit IgG
• guinea pig IgG
• rat IgG
• goat IgG
• sheep IgG
• cow IgG
• horse IgG
Recombinant protein G does not bind to IgG from chicken or cat, or to human IgA, IgM, or serum albumin. It binds weakly to IgG from dog.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
FormSuspension
Quantity2 mL
Column TypeAffinity
Product LineSepharose
Product TypeProtein G Sepharose
Stationary PhaseProtein G
Unit SizeEach
Contents & Storage
This product is supplied as a 50% suspension (2 ml Recombinant Protein G-Sepharose™ 4B + 2 ml PBS) Wet Ice
Frequently asked questions (FAQs)
Can I perform a centrifugation separation with Recombinant Protein G - Sepharose 4B (Cat. Nos. 101241, 101242, 101243) instead of column separation?
Citations & References (4)
Citations & References
Abstract
Inducible T cell antigen 4-1BB. Analysis of expression and function.
Journal:J Immunol
PubMed ID:7678621
'4-1BB is an inducible receptor-like protein expressed in both cytolytic and Th cells. Optimal induction of 4-1BB mRNA in T cells required both PMA and ionomycin stimulation, indicating that protein kinase C activation and increases in intracellular Ca2+ were required for its expression. 4-1BB was categorized as an early activation
The glycosylation of IgA produced by murine B cells is altered by Th2 cytokines.
Journal:J Immunol
PubMed ID:9278322
'We sought to determine whether selected cytokines, known to profoundly increase proliferation and/or production of Ig by B cells and their progeny, also have as yet unrecognized effects upon IgA glycosylation. For these studies, we selected CH12LX mouse B lymphoma cells, a widely used model of B cell differentiation. Glycosylation
A knock-in mouse model of gastrointestinal stromal tumor harboring kit K641E.
Journal:Cancer Res
PubMed ID:16061643
A mouse model of gastrointestinal stromal tumor (GIST) has been developed by a knock-in gene targeting strategy, which introduced a Kit gene K641E mutation, originally identified in sporadic human GISTs and in the germ line of familial GIST syndrome patients. Homozygous and heterozygous Kit K641E mice develop gastrointestinal pathology with
Targeting the intracellular MUC1 C-terminal domain inhibits proliferation and estrogen receptor transcriptional activity in lung adenocarcinoma cells.
Journal:Mol Cancer Ther
PubMed ID:21862684
Mucin 1 (MUC1) is a diagnostic factor and therapy target in lung adenocarcinoma. MUC1 C-terminal intracellular domain (CD) interacts with estrogen receptor (ER) a and increases gene transcription in breast cancer cells. Because lung adenocarcinoma cells express functional ERa and ERß, we examined MUC1 expression and MUC1-ER interaction. Because blocking