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14-314M Syk Protein, active, 250 µg

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14-314M
250 µg  Also available in 10 μg size (cat#14-314) and in bulk (cat# 14-314-K).
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      Overview

      Replacement Information
      Description
      Catalogue Number14-314M
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionSyk Protein, active, 250 µg
      OverviewRecombinant full-length human Syk, containing an N-terminal His6-tag
      References
      Product Information
      Quality LevelMQ100
      Applications
      ApplicationActive, recombinant full-length human Syk, containing an N-terminal His6-tag, for use in Kinase Assays.
      Key Applications
      • Kinase Assay
      Biological Information
      SourceExpressed by baculovirus in Sf21 insect cells
      Specific ActivityFor Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
      Entrez Gene Number
      Gene Symbol
      • SYK
      Protein TargetSyk
      Purification MethodNi2+/NTA-agarose
      Target Sub-FamilyTK
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P43405 # Positive effector of BCR-stimulated responses. Couples the B-cell antigen receptor (BCR) to the mobilization of calcium ion either through a phosphoinositide 3-kinase-dependent pathway, when not phosphorylated on tyrosines of the linker region, or through a phospholipase C-gamma-dependent pathway, when phosphorylated on Tyr-348 and Tyr-352. Thus the differential phosphorylation of Syk can determine the pathway by which BCR is coupled to the regulation of intracellular calcium ion (By similarity).
      SIZE: 635 amino acids; 72066 Da
      SUBUNIT: Interacts with CBL and SLA when it is phosphorylated. The interaction with SLA may link it to CBL, leading to its destruction. Interacts with phosphorylated NFAM1 (By similarity). Interacts with Epstein-Barr virus LMP2A. Interacts through its SH2 domains with the phosphorylated ITAM domain of CD79A which stimulates SYK autophosphorylation and activation.
      PTM: Autophosphorylated. & Phosphorylation on Tyr-323 creates a binding site for c-Cbl, an adapter protein that serves as a negative regulator of BCR- stimulated calcium ion signaling (By similarity). & Phosphorylation on Tyr-348 and Tyr-352 enhances the phosphorylation and activation of phospholipase C-gamma and the early phase of calcium ion mobilization via a phosphoinositide 3- kinase-independent pathway (By similarity). & Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation (By similarity).
      SIMILARITY: SwissProt: P43405 ## Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily. & Contains 1 protein kinase domain. & Contains 2 SH2 domains.
      Molecular Weight73kDa
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality Assuranceroutinely evaluated by phosphorylation of Poly (Glu4-Tyr)
      Usage Statement
      • 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.
      Storage and Shipping Information
      Storage Conditions1 year at -70C
      Packaging Information
      Material Size250 µg
      Material PackageAlso available in 10 μg size (cat#14-314) and in bulk (cat# 14-314-K).
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      14-314M 04053252583841

      Related Products & Applications

      Alternative Packsize

      Catalogue Number Description  
      14-314 Syk Protein, active, 10 µg Show Pricing & Availability

      Product Families

      Categories

      Life Science Research > Proteins and Enzymes > Purified Kinases
      Life Science Research > Drug Discovery and Development > Kinase & Phosphatase Screening > Purified Kinases