Hck (E1I7F) Rabbit mAb #14643

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Supporting Data

REACTIVITY	H
SENSITIVITY	Endogenous
MW (kDa)	59, 61
Source/Isotype	Rabbit IgG

Application Key:

WB-Western Blotting
IP-Immunoprecipitation

Species Cross-Reactivity Key:

H-Human

Product Information

Product Usage Information

Application	Dilution
Western Blotting	1:1000
Immunoprecipitation	1:100

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Hck (E1I7F) Rabbit mAb recognizes endogenous levels of total Hck protein.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys60 of human Hck protein.

Background

The hematopoietic cell kinase (Hck) is a Src family protein tyrosine kinase that is prominently expressed in lymphoid and myeloid lineages of hematopoiesis (1). The Hck kinase participates in transduction of a variety of extracellular signals that affect cellular processes, including cell proliferation, differentiation, and migration. Hck protein structure includes a relatively divergent amino-terminal "unique" domain that is subject to post-translational lipid modifications and targets Hck to the plasma membrane. Src homology 3 (SH3) and 2 (SH2) domains, and a tyrosine kinase catalytic domain are adjacent to the "unique" domain. Research studies indicate that phosphorylation of conserved tyrosine residues positively and negatively regulate Hck catalytic activity. Phosphorylation of Hck at the conserved, carboxy-terminal Tyr499 by protein kinase Csk promotes an interaction between the phosphorylated tyrosine and the SH2 domain, rendering Hck inactive. Disruption of this interaction through dephosphorylation, the replacement of the Tyr522 with phenylalanine, or carboxy-terminal truncation mutations, results in constitutive activation of Hck. Autophosphorylation of Tyr411 within the kinase domain positively regulates Hck catalytic activity. Thus, the activation of Hck requires both disruption of the regulatory tyrosine-SH2 domain interaction and autophosphorylation of the regulatory tyrosine residue within the kinase domain (2,3). The dysfunction or dysregulation of Hck may contribute to the pathogenesis of some human forms of leukemia (4).

Database Links

UniProt ID: P08631

Entrez-Gene Id: 3055

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For Research Use Only. Not For Use In Diagnostic Procedures.

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