DUSP19 Antibody Blocking Peptide(bs-14454P)-500ug

DUSP19 Antibody Blocking Pepti

de(bs-14454P)-500ug
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  • bs-14454P
  • 2025年10月16日
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      500ug

    产品编号bs-14454P
    英文名称DUSP19 Antibody Blocking Peptide
    中文名称双特异性磷酸酶封闭多肽19封闭多肽
    英文别名Dual specificity phosphatase 19; Dual specificity phosphatase TS DSP1; Dual specificity phosphatase TS-DSP1; Dual specificity protein phosphatase 19; DUS19_HUMAN; DUSP 17; DUSP 19; DUSP17; Dusp19; LMW DSP3; LMW-DSP3; LMWDSP 3; LMWDSP3; Low molecular weight dual specificity phosphatase 3; MGC138210; Protein phosphatase SKRP1; SAPK pathway regulating phosphatase 1; SAPK pathway-regulating phosphatase 1; SKRP 1; SKRP1; Stress activated protein kinase pathway regulating phosphatase 1; Stress-activated protein kinase pathway-regulating phosphatase 1; TS DSP1.
    纯化方法HPLC
    组织特异性Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest.
    相似性Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
    Contains 1 tyrosine-protein phosphatase domain.
    功能Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    注意事项This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
    背景资料Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]

     

     

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