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HNRNPUL1 Recombinant monoclonal antibody, PBS Only

HNRNPUL1 Uni-rAb® Recombinant Antibody for WB, Indirect ELISA

Cat No. 86926-3-PBS
Clone No.252010C1

Host / Isotype

Rabbit / IgG

Reactivity

human, mouse, rat

Applications

WB, Indirect ELISA

Adenovirus early region 1B-associated protein 5, E1B AP5, E1B-55 kDa-associated protein 5, E1BAP5, E1B-AP5

Formulation:  PBS Only
Conjugate:  Unconjugated
Size/Concentration: 

-/ -

Freight/Packing: -

Quantity

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Product Information

86926-3-PBS targets HNRNPUL1 in WB, Indirect ELISA applications and shows reactivity with human, mouse, rat samples.

Tested Reactivity human, mouse, rat
Host / Isotype Rabbit / IgG
Class Recombinant
Type Antibody
Immunogen

CatNo: Ag0899

Product name: Recombinant human HNRNPUL1 protein

Source: e coli.-derived, PGEX-4T

Tag: GST

Domain: 1-227 aa of BC002564

Sequence: MDVRRLKVNELREELQRRGLDTRGLKAELAERLQAALEAEEPDDERELDADDEPGRPGHINEEVETEGGSELEGTAQPPPPGLQPHAEPGCYSGPDGHYAMDNITRQNQFYDTQVIKQENESGYERRPLEMEQQQAYRPEMKTEMKQGAPTSFLPPEASQLKPDRQQFQSRKRPYEENRGRGYFEHREDRRGRSPQPPAEEDEDDFDDTLVAIDTYNCDLHFKVARD

Predict reactive species
Full Name heterogeneous nuclear ribonucleoprotein U-like 1
Calculated Molecular Weight 120 kDa
Observed Molecular Weight120 kDa
GenBank Accession NumberBC002564
Gene Symbol HNRNPUL1
Gene ID (NCBI) 11100
RRIDAB_3745210
Conjugate Unconjugated
FormLiquid
Purification MethodProtein A purification
UNIPROT IDQ9BUJ2
Storage Buffer PBS only, pH 7.3.
Storage ConditionsStore at -80°C.

Background Information

HNRNPUL1, also named as E1BAP5, HNRPUL1 and E1B-AP5, acts as a basic transcriptional regulator. It represses basic transcription driven by several virus and cellular promoters. HNRNPUL1 plays also a role in mRNA processing and transport. It is a cellular protein that interacts with the adenovirus protein E1B-55 and implicated in mRNA export. HNRNPUL1 is an hnRNP-like protein that likely mediates the interaction of NXF1 with mRNAs.(PMID:17267598). It may modulate PAN expression in complex with KSHV ORF57(PMID:22043172). HNRNPUL1 specifically bound to the Rae1-Nup98 complex independently of M protein, and this interaction was found to be RNA dependent, as it was greatly diminished in the presence of RNase.

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