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Anti-Unrip/STRAP Antibody Picoband® Fluoro488 Conjugated

Product Specifications

Background

Unrip is also known as STRAP (Serine-threonine kinase receptor-associated protein) . It is anenzyme that in humans is encoded by the STRAP gene. It is mapped to 12p12.3. UNRIP is integrated into a complex with UNR or with the SMN complex in vivo in a mutually exclusive manner. It is concluded that UNRIP is the first component of the uridine-rich snRNP assembly machinery that associates with the SMN complex in a compartment-specific way, and it may play a crucial role in the intracellular distribution of the SMN complex.

Synonyms

Serine-threonine kinase receptor-associated protein; MAP activator with WD repeats; UNR-interacting protein; WD-40 repeat protein PT-WD; STRAP; MAWD, UNRIP

Gene Name

STRAP

Gene ID

11171

UniProt

Q9Y3F4

Host

Rabbit

Reactivity

Human, Mouse, Rat

Cross Reactivity

No cross-reactivity with other proteins.

Immunogen

A synthetic peptide corresponding to a sequence at the N-terminus of human Unrip, identical to the related mouse and rat sequences.

Clonality

Polyclonal

Tissue Specificity

Ubiquitously expressed in various human primary cells and tumor cell lines. .

Applications

Flow Cytometry

Field of Research

Chaperones, Protein Trafficking, Signal Transduction

Purification

Immunogen affinity purified.

Form

Liquid

Function

The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. .

References & Citations

1. Datta PK, Chytil A, Gorska AE, Moses HL (December 1998) . Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling. J. Biol. Chem. 273 (52) : 34671–4. 2. Grimmler, M., Otter, S., Peter, C., Muller, F., Chari, A., Fischer, U. Unrip, a factor implicated in cap-independent translation, associates with the cytosolic SMN complex and influences its intracellular localization. Hum. Molec. Genet. 14: 3099-3111, 2005.

Storage Conditions

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

Product Datasheet

https://www.bosterbio.com/datasheet?sku=PB9407-Fluoro488

Calculated Molecular Weight

38438 MW

Specificity

No cross reactivity with other proteins.

Applications Notes

6

Gene Name Synonym

Serine-threonine kinase receptor-associated protein

Subcellular Location

Cytoplasm. Nucleus. Localized predominantly in the cytoplasm but also found in the nucleus.

Sequence Similarities

Belongs to the WD repeat STRAP family.

Protein Name

Serine-threonine kinase receptor-associated protein

Isotype

Rabbit IgG

Contents

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.

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