Skip to Content
MilliporeSigma
All Photos(1)

Key Documents

08062

Sigma-Aldrich

Protein G′ from Streptococcus sp.

recombinant, expressed in E. coli

Synonym(s):

IgG F(c)-Receptor

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.26

biological source

bacterial (Streptococcus sp.)

Quality Level

recombinant

expressed in E. coli

form

lyophilized solid

mol wt

~30 kDa

capacity

~5 mg/mg, solid binding capacity (IgG)

storage temp.

−20°C

General description

Protein G, a cell wall protein, is obtained from group G streptococci. The extracellular part of this protein is made of two/three small domains or serum albumin binding (GA domains) and two/three immunoglobulin (IgG) binding domains (B domains).
Genetically engineered truncated protein G; retains affinity for IgG, but lacks albumin and Fab binding sites and membrane-binding regions.

Application

Protein G′ from Streptococcus sp. has been used in in vitro actin labeling assay.

Biochem/physiol Actions

Protein G can bind all the human and mouse IgG subclasses. It can bind to both the fragment crystallizable (Fc) and antigen-binding fragment (Fab) components of the antibody.

Physical form

lyophilized powder in a Tris-HCl buffer, pH 7.5

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Essential Guides for Isolation/Purification of Immunoglobulins
Layer A, et al.
Encyclopedia of Separation Science, 4553-4559 (2000)
1405830
Nezlin R
The Immunoglobulins: Structure and Function null
Archana Kumari et al.
The EMBO journal, 39(14), e104006-e104006 (2020-06-23)
Cellular studies of filamentous actin (F-actin) processes commonly utilize fluorescent versions of toxins, peptides, and proteins that bind actin. While the choice of these markers has been largely based on availability and ease, there is a severe dearth of structural

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service