Cet anticorps Lapin Polyclonal détecte spécifiquement DRAK2 dans ELISA, WB, IHC et IF. Il présente une réactivité avec des échantillons de Humain, Souris et Rat.
STK17B
Reactivité: Humain
WB, IF, EIA
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
Optimal working dilutions should be determined experimentally by the investigator. Suggested starting dilutions are as follows: WB 1:500-1:2000,IHC 1:100-1:300,ELISA 1:40000,IF 1:50-200
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
Liquid in PBS containing 50 % glycerol, 0.5 % BSA and 0.02 % sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
-20 °C
Stockage commentaire
Stable for one year at -20°C from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquot to avoid repeated freezing and thawing.
STK17B, DRAK2, Serine/threonine-protein kinase 17B, DAP kinase-related apoptosis-inducing protein kinase 2DAP (death associated protein) kinase and ZIP kinase are members of a novel protein kinase family, the members of which have the capacity to mediate apoptosis through their catalytic activities. DAP kinase contains a "death domain" and has been shown to mediate gamma interferon-induced apoptosis. The introduction of DAP kinase into highly metastatic carcinoma clones lacking DAP kinase expression was shown to result in the suppression of metastasis, thus linking suppression of apoptosis to metastasis. ZIP kinase contains a leucine zipper domain, which is necessary for homodimerization and for interaction with other leucine zipper proteins. ZIP kinase dimerizes with ATF-4, an ATF/CREB transcription factor family member that contains a leucine zipper. DRAK1 (DAP kinase-related apoptosis-inducing protein kinase 1) and DRAK2 are DAP kinase related proteins. DRAK1 and DRAK2 are localized to the nucleus, and overexpression of both DRAK proteins in NIH/3T3 cells induces morphological changes associated with apoptosis.