anti-phospho-cdc37 (ser13) rabbit pab

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Anti-Phospho-Cdc37 (Ser13) Rabbit pAb Clone Number: – Host: Rabbit Clonality: Polyclonal Applications： WB Reactivity: Human, Rat Synonyms: Hsp90 co-chaperone Cdc37, p50Cdc37, CDC37A Product Size 100 μl ADD TO CART BUY NOW Quantity Shipping: Ambient temperature Order online or send purchase order to [email protected] FAQ Technical Support Protocols General Information Product Usage Information Properties Target Information Images Recommended Products References BUY NOW General Information Isotype IgG Conjugate Unconjugated Synonyms Hsp90 co-chaperone Cdc37, p50Cdc37, CDC37A UniProt ID Q16543 Immunogen MW (kDa) Specificity Product Usage Information Applications Dilution Recommended Species WB 1:500 – 1:2000 Human, Rat Properties Purity Protein A purified Constituents PBS, Glycerol, BSA Storage Store at -20°C. Avoid freeze/thaw cycles. Stability Stable for 12 months from date of receipt/reconstitution. Target Information Background CDC37 is an important component of the HSP90 chaperone complex. It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins. CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation. CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading. CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways. Moreover, CDC37 is phosphorylated by CKII at its carboxy-terminal Ser13 residue, which is required for its interaction with HSP90 and target protein stabilization function. Cellular location Cytoplasm, Nucleus Images WB Blocking buffer: 5% NFDM/TBSTPrimary Ab dilution: 1:2000 Primary Ab incubation condition: 2hoursat room temperature Secondary Ab: Goat Anti-Rabbit IgGH&L(HRP Conjugate) Lysate: (-): HeLa, (+): HeLa + OkadaicA(100nM,60min) + Calyculin A (100nM,60min) Protein loading quantity: 20 μg Exposure time: 30 secondsPredicted band size: 50 kDaObserved band size: 50 kDa Blocking buffer: 5% NFDM/TBSTPrimary Ab dilution: 1:2000 Primary Ab incubation condition: 2hoursat room temperature Secondary Ab: Goat Anti-Rabbit IgGH&L(HRP Conjugate) Lysate: -): C6, (+): C6 + CalyculinA(100nM, 30min) Protein loading quantity: 20 μg Exposure time: 30 secondsPredicted band size: 50 kDa Observed band size: 50 kDa :
Anti-Phospho-Cdc37 (Ser13) Rabbit pAb Clone Number: – Host: Rabbit Clonality: Polyclonal Applications： WB Reactivity: Human, Rat Synonyms: Hsp90 co-chaperone Cdc37, p50Cdc37, CDC37A Product Size 100 μl ADD TO CART BUY NOW Quantity Shipping: Ambient temperature Order online or send purchase order to [email protected] FAQ Technical Support Protocols General Information Product Usage Information Properties Target Information Images Recommended Products References BUY NOW General Information Isotype IgG Conjugate Unconjugated Synonyms Hsp90 co-chaperone Cdc37, p50Cdc37, CDC37A UniProt ID Q16543 Immunogen MW (kDa) Specificity Product Usage Information Applications Dilution Recommended Species WB 1:500 – 1:2000 Human, Rat Properties Purity Protein A purified Constituents PBS, Glycerol, BSA Storage Store at -20°C. Avoid freeze/thaw cycles. Stability Stable for 12 months from date of receipt/reconstitution. Target Information Background CDC37 is an important component of the HSP90 chaperone complex. It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins. CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation. CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading. CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways. Moreover, CDC37 is phosphorylated by CKII at its carboxy-terminal Ser13 residue, which is required for its interaction with HSP90 and target protein stabilization function. Cellular location Cytoplasm, Nucleus Images WB Blocking buffer: 5% NFDM/TBSTPrimary Ab dilution: 1:2000 Primary Ab incubation condition: 2hoursat room temperature Secondary Ab: Goat Anti-Rabbit IgGH&L(HRP Conjugate) Lysate: (-): HeLa, (+): HeLa + OkadaicA(100nM,60min) + Calyculin A (100nM,60min) Protein loading quantity: 20 μg Exposure time: 30 secondsPredicted band size: 50 kDaObserved band size: 50 kDa Blocking buffer: 5% NFDM/TBSTPrimary Ab dilution: 1:2000 Primary Ab incubation condition: 2hoursat room temperature Secondary Ab: Goat Anti-Rabbit IgGH&L(HRP Conjugate) Lysate: -): C6, (+): C6 + CalyculinA(100nM, 30min) Protein loading quantity: 20 μg Exposure time: 30 secondsPredicted band size: 50 kDa Observed band size: 50 kDa