Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • ELISA
  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.

News

Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

Exalpha Biologicals, Inc.

phospho c-Abl [pY245]

  • Product Code: X2014P
  • Size: 10 µg
  • Price (USD): $562

Cat #

X2014P		 Quantity:      

Data Sheet

Product Name

phospho c- Abl [pY245]

Host/Source

Rabbit

Clone

Polyclonal

Product Type

Phosphorylation Site-Specific Antibody

Reactivity

Human

Applications

Western Blot

Purification

Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated c-Abl. The final product is generated by affinity chromatography using a c-Abl -derived peptide that is phosphorylated at tyrosine 245.

Size

10 µg

Price (USD)

$562

Background

c-Abl is a 140-150 kDa non-receptor protein tyrosine kinase whose precise functions are not known, but roles for Abl in growth factor and integrin signaling, cell cycle regulation, cytoskeletal reorganization, neurogenesis, and responses to DNA damage and oxidative stress have been suggested. c-Abl kinase activity is increased in vivo by diverse physiological stimuli including ionizing radiation, entry into S phase, integrin activation, and platelet-derived growth factor (PDGF) stimulation. c-Abl contains various protein binding domains that appear to enable it to regulate the functions of many proteins by forming complexes, most notably three isoforms of the oncogenic protein BCR/ABL. Tyrosine 245 is involved in the activation of c-Abl kinase activity, and phosphorylated by Src after PDGF stimulation.

Immunogen

The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of human c-Abl that contains tyrosine 245. Note: there are two widely expressed forms of c-Abl produced by alternative splicing, known as 1a and 1b (the more commonly used form). The corresponding phosphorylation site from 1a is tyrosine 226.

Positive Control

Fibroblasts transfected with oncogenic ΔSH3-Abl.

Formulation

Provided as solution in phosphate buffered saline, pH 7.3, with 1% BSA and 0.08% sodium azide

Customer Storage

Product should be stored at -80°C. Aliquot to avoid freeze/thaw cycles

Target Molecular Weight

140 kDa

Database Links:

SwissProtA3KFJ3Human

References

1. Cong, F., et al. (2002) Interaction between UV-damaged DNA binding activity proteins and the c-Abl tyrosine kinase. J. Biol. Chem. 277(38):34870-34878.
2. Furstoss, O., et al. (2002) c-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis. EMBO J. 21(4):514-524.
3. Brasher, B.B. and R.A. Van Etten (2000) c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines. J. Biol. Chem. 275(45):35631-35637.
4. Plattner, R., et al. (1999) c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13(18):2400-2411.