recommended for detection of TRIM10 of human origin by WB, IP and ELISA
Modification Notes
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM10, also known as RING finger protein 9, RFB30 or HERF1, is a 481 amino acid protein that localizes to the cytoplasm. Expressed exclusively in hematopoetic tissues that contain developing myeloid, erythroid or megakaryocytic progenitors, TRIM10 has been shown to play a critical role in the terminal differentiation of erythroid cells. The functions of the various domains in TRIM10 suggest a role in the regulation of transcriptional signaling as well a mechanistic role in the morphological changes that occur during erythroid development. The expression of TRIM10 is dependent on upstream effectors such as PEBP2∫ and PU.1. Two named isoforms of TRIM10 exist as a result of alternative splicing events.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
WB:1:500~1:2000 IP:1:100~1:500 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of TRIM10 of human origin by WB IP and ELISA
Tissue Specificity
recommended for detection of TRIM10 of human origin by WB, IP and ELISA