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TRIM69 polyclonal Antibody | BS7914

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BW-BS7914
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NULL444.00 - NULL678.00

Description

TRIM69 polyclonal Antibody | BS7914 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human,Mouse,Rat

Application: WB IHC IF

Application Range: WB: 1:500~1:2000 IHC/IF: 1:50~1:200

Background: 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. TRIM69 (tripartite motif-containing 69), also known as Trif, HSD34 or RNF36 (RING finger protein 36), is a 500 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger and one B30.2/SPRY domain. Localizing to nuclear speckles, TRIM69 interacts with PML (promyelocytic leukemia) and is thought to play a role in spermatogenesis and, when overexpressed, may be involved in apoptosis. TRIM69 is subject to posttranslational phosphorylation, an event which is necessary for TRIM69 nuclear localization. Multiple isoforms of TRIM69 exist due to alternative splicing events.

Storage & Stability: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Specificity: TRIM69 polyclonal Antibody detects endogenous levels of TRIM69 protein.

Molecular Weight: ~ 57 kDa

Note: For research use only, not for use in diagnostic procedure.

Alternative Names: E3 ubiquitin protein ligase TRIM69; HSD34; RFP like domain containing protein trimless; RFP-like domain-containing protein trimless; RING finger protein 36; RNF36; TRI69_HUMAN; Trif; Trim69; Trimless; Tripartite motif containing 69; tripartite motif containing protein 69; tripartite motif protein 69; Tripartite motif-containing protein 69;

Immunogen: Recombinant full length Human TRIM69.

Conjugate: Unconjugated

Modification: Unmodification

Purification & Purity: The Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Pathway:

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