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Purified Mouse Anti-PKCλ
Product Details
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BD Transduction Laboratories™
Rat (QC Testing), Human, Mouse, Dog, Chicken (Tested in Development)
Mouse IgG1
Human PKCλ aa. 397-558
Western blot (Routinely Tested), Immunofluorescence, Immunohistochemistry, Immunoprecipitation (Tested During Development)
74 kDa
250 µg/ml
AB_397606
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
610208 Rev. 3
Antibody Details
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41/PKCλ

The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases is involved in a number of processes such as growth, differentiation, and cytokine secretion. At least eleven isozymes have been described. These proteins are products of multiple genes and alternative splicing. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half containing C1, C2, V1, and V2 constitutes the regulatory domain and interacts with the PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester. However, the novel PKC (nPKC) subfamily members ( δ, ε, η, and θ isoforms) and the atypical PKC (aPKC) subfamily members (ζ, ί, and λ isoforms) are Ca2+ independent and lack the C2 domain. The aPKC members are unique in that their activity is independent of diacylglycerols and phorbol esters. They also lack one repeat of the cysteine-rich sequences that are conserved in cPKC and nPKC. The C-terminal region of PKC contains the catalytic domain. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters, and growth factors. PKCλ shows the highest degree of amino acid homology with PKCζ (72%) and PKCλ mRNA is expressed in a variety of cells and tissues. The PKCλ protein kinase is capable of autophosphorylation and can be activated by phosphatidylserine, but not by other PKC activators such as diacylglycerols, Ca2+, or phorbol esters.

610208 Rev. 3
Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
610208 Rev.3
Citations & References
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Development References (5)

  1. Akimoto K, Mizuno K, Osada S. A new member of the third class in the protein kinase C family, PKC lambda, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells. J Biol Chem. 1994; 269(17):12677-12683. (Biology). View Reference
  2. Jain N, Zhang T, Kee WH, Li W, Cao X. Protein kinase C delta associates with and phosphorylates Stat3 in an interleukin-6-dependent manner. J Biol Chem. 1999; 274(34):24392-24400. (Clone-specific: Immunoprecipitation, Western blot). View Reference
  3. Pauken CM, Capco DG. The expression and stage-specific localization of protein kinase C isotypes during mouse preimplantation development. Dev Biol. 2000; 223(2):411-421. (Clone-specific: Immunofluorescence, Western blot). View Reference
  4. Trauzold A, Wermann H, Arlt A. CD95 and TRAIL receptor-mediated activation of protein kinase C and NF-kappaB contributes to apoptosis resistance in ductal pancreatic adenocarcinoma cells. Oncogene. 2001; 20(31):4258-4269. (Clone-specific: Western blot). View Reference
  5. Uberall F, Giselbrecht S, Hellbert K. Conventional PKC-alpha, novel PKC-epsilon and PKC-theta, but not atypical PKC-lambda are MARCKS kinases in intact NIH 3T3 fibroblasts. J Biol Chem. 1997; 272(7):4072-4078. (Clone-specific: In vitro kinase assay). View Reference
View All (5) View Less
610208 Rev. 3

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For Research Use Only. Not for use in diagnostic or therapeutic procedures.