Exalpha Biologicals, Inc.

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FIX&PERM Cell Fixation and Permeabilization Kit

Flow cytometric analyses with monoclonal antibodies were so far mainly restricted to cell surface molecules. Intracellular structures such as cytoplasmic or nuclear enzymes, oncoproteins, cytokines, immunoglobulins etc. were largely excluded from such studies. Also excluded from flow cytometric studies were cytoplasmic localizations of well-established membrane molecules like CD3 and CD22, which, in their cytoplasmic form, are the most reliable lineage markers in undifferentiated leukemia. With the FIX&PERM® Kit flow cytometric analysis of intracellular antigens has become as easy as surface antigen studies. The only prerequisite is the availability of suitable antibody conjugates. Most of the available monoclonal antibody conjugates can be used with the FIX&PERM® Kit, some determinants are sensitive, however, to the fixation step involved. This and the optimal fixation time have to be tested for each reagent.


Welcome, Peter Rutten

We are pleased to announce that Peter Rutten has now started in his role as Operations Director here at Exalpha Biologicals Inc. Peter has a Master’s of Science degree in Industrial and Organizational Psychology and this has lead him down a very business orientated career path. Peter is looking forward to working with the team at Exalpha. Peters primary focus is the customer experience and he will be working with the Laboratory team, the Quality Control team and the Order Processing team to ensure this focus is achieved. We all wish Peter well in his new role.

Exalpha Biologicals, Inc.

phospho c-Abl [pY245]

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

Cat #

X2014P		 Quantity:      

Data Sheet

Product Name

phospho c- Abl [pY245]





Product Type

Phosphorylation Site-Specific Antibody




Western Blot


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.


10 µg

Price (USD)



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.


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 SH3-Abl.


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:



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.