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G2791

Sigma-Aldrich

Anti-Grb-2 antibody, Mouse monoclonal

clone GRB-232, purified from hybridoma cell culture

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About This Item

MDL number:
MFCD00802742
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

GRB-232, monoclonal

form

buffered aqueous solution

mol wt

antigen 24 kDa

species reactivity

rat, mouse, human

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using a whole extract of cultured human acute T-cell leukemia Jurkat cells

isotype

IgG3

UniProt accession no.

P62993

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GRB2(2885)
mouse ... Grb2(14784)
rat ... Grb2(81504)

General description

Grb2 is an adapter protein with one Src homology 2 (SH2) domain and two SH3 domains that facilitate protein-protein interactions. grb2 is highly conserved across species and is critical for development events such as epithelial morphogenesis, cell motility and vasculogenesis. Grb2 is closely associated with Sos and activates Ras and the MAPK cascade. Grb2 interacts with signalling proteins involved in T-cell development, B-cell activation and development and autoimmunity. Recent reports implicates Grb2 role in several oncogenic signalling pathways that lead to CML and breast cancer.
Monoclonal Anti-Grb2 reacts specifically with Grb2 (24 kDa).

Immunogen

synthetic peptide (a.a. 200-217) corresponding to the C-terminal region of human, rat and mouse Grb2.

Application

Anti-Grb-2 antibody may be used at a working concentration of 1-2 μg/mL for detection by immunoblotting in whole cell extracts of human T cell leukemia, Jurkat cells. Detection is also possible in extracts of murine spermatozoa by immunoblotting at a working dilution of 1:1000. The antibody is suitable for indirect ELISA, immunocytochemistry, immunohistochemistry, immunoprecipitation and protein microarray.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Preparation Note

Purified from culture supernatant of hybridoma cells grown in a bioreactor.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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A M Pendergast et al.
Cell, 75(1), 175-185 (1993-10-08)
BCR-ABL is a chimeric oncoprotein that exhibits deregulated tyrosine kinase activity and is implicated in the pathogenesis of Philadelphia chromosome (Ph1)-positive human leukemias. Sequences within the first exon of BCR are required to activate the transforming potential of BCR-ABL. The
R J Daly et al.
Oncogene, 9(9), 2723-2727 (1994-09-01)
A receptor blotting technique was used to detect SH2 domain containing epidermal growth factor receptor (EGFR) substrates that exhibited differential expression either between normal breast epithelial cells and breast cancer cells or between different human breast cancer cell lines. This
Arif Yurdagul et al.
Journal of cell science, 129(8), 1580-1591 (2016-02-26)
Oxidized low-density lipoprotein (oxLDL) accumulates early in atherosclerosis and promotes endothelial nuclear factor κB (NF-κB) activation, proinflammatory gene expression and monocyte adhesion. Like for other atherogenic factors, oxLDL-induced proinflammatory responses requires integrin-dependent focal adhesion kinase (FAK, also known as PTK2)
B-cell positive selection and peripheral homeostasis.
John G Monroe
Immunological reviews, 197, 5-9 (2004-02-14)
A M Tari et al.
Seminars in oncology, 28(5 Suppl 16), 142-147 (2001-11-14)
The growth factor receptor-bound protein-2 (GRB2) is essential for multiple cellular functions. Inhibition of GRB2 function impairs developmental processes in various organisms and blocks transformation and proliferation of various cell types. GRB2 is most well known for its ability to
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