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06-583

Sigma-Aldrich

Anti-Lck Antibody

Upstate®, from rabbit

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

packaging

antibody small pack of 25 μg

manufacturer/tradename

Upstate®

technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... LCK(3932)

General description

Tyrosine-protein kinase Lck (UniProt: P06239; also known a EC:2.7.10.2, Leukocyte C-terminal Src kinase, LSK, Lymphocyte cell-specific protein-tyrosine kinase, Protein YT16, Proto-oncogene Lck, T cell-specific protein-tyrosine kinase, p56-LCK) is encoded by the LCK gene (Gene ID: 3932) in human. Lck is a non-receptor tyrosine kinase that is specifically expressed in lymphoid cells. Its protein kinase domain is localized to amino acids 245-498. It plays an essential role in the selection and maturation of developing T-cells in the thymus and also plays a role in function of mature T-cells. It is reported to constitutively associate with the cytoplasmic region of the CD4 and CD8 receptors. It also plays a role in T-cell antigen receptor (TCR)-linked signaling. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively. This results in recruitment of Lck to the vicinity of the TCR/CD3 complex where Lck can phosphorylate tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR- chains and CD3 subunits that initiates the TCR/CD3 signaling. Once stimulated, the TCR recruits the tyrosine kinase ZAP70 that becomes phosphorylated and activated by Lck. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. Autophosphorylation of Lck on tyrosine 394 increases its enzyme activity, whereas phosphorylation on tyrosine 505 by C-terminal Src kinase (CSK) results in a reduction in its activity. (Ref.: Rossy, J., et al. (2012). Front. Immunol. 3; 167; Bergman, M., et al. (1992). EMBO J. 11(8); 2919-2924).

Specificity

This rabbit polyclonal antibody detects Tyrosine-protein kinase Lck. It targets an epitope within the N-terminal region.

Immunogen

GST-tagged recombinant fragment corresponding to the first 58 amino acids from the N-terminal region of human Tyrosine-protein kinase Lck.

Application

Quality Control Testing

Evaluated by Western Blotting in Jurkat cell lysate.Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Lck in Jurkat cell lysate.Tested Applications

Immunoprecipitation Analysis: A representative lot immunoprecipitated Lck in Jurkat cell lysate.Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

Quality

routinely evaluated by immunoblot on RIPA lysates from Jurkat cells

Target description

~56 kDa observed; 58.0 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Linkage

Replaces: 04-372

Physical form

Format: Purified
Protein A chromatography
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Store at -10°C to -25°C. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Analysis Note

Control
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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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Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies.
Banerji, U; O'Donnell, A; Scurr, M; Pacey, S; Stapleton, S; Asad, Y; Simmons, L; Maloney et al.
Journal of clinical oncology : official journal of the American Society of Clinical Oncology null
S Shin et al.
Oncogene, 8(1), 141-149 (1993-01-01)
We have analysed DNA and RNA from 36 T-cell lymphomas induced in Fischer rats by Moloney murine leukemia virus for alterations affecting the structure or expression of the lck gene. At least five primary tumors (14%) have a proviral insertion
R S Lin et al.
The Journal of biological chemistry, 273(49), 32878-32882 (1998-11-26)
Binding of the protein tyrosine kinase p56(lck) to T-cell co-receptors CD4 and CD8alpha is necessary for T-lymphocyte development and activation. Association of p56(lck) with CD4 requires two conserved cysteine residues in the cytosolic domain of CD4 and two in the
E Rouer et al.
Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research, 5(6), 659-666 (1994-06-01)
The lck gene encodes a tyrosine protein kinase of the src family which is highly expressed in T-lymphocytes. Two widely separated promoters govern expression of the lck gene. We report in this study that alternative splicing between cryptic donor and
Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models.
Banerji, U; Walton, M; Raynaud, F; Grimshaw, R; Kelland, L; Valenti, M; Judson, I; Workman, P
Clinical cancer research : an official journal of the American Association for Cancer Research null

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