Tgfbr1; ALK5; Alk-5; TbetaRI; AU017191; TbetaR-I

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 4; NC_000070.6 (47352312..47414926). Location: 4 B1; 4 26.02 cM

Monoclonal

IgG2

3A11

Rat

This antibody recognizes mouse ALK5 in western blot. Cross reactivity to other species have not been tested!

Protein G chromatography

Lyophilized

Lyophilized samples are stable for 2 years from date of receipt when stored at -70 degree C. Reconstituted antibody can be aliquoted and stored frozen at < -20 degree C for at least for six months without detectable loss of activity.
Shipping: ships RT or 4 degree C.

Manufactured in an ISO 9001:2008 Certified Laboratory.

Small volumes of anti-ALK-5 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Most cell types express three sizes of receptors for TGFbeta. These are designated Type I (53 kDa), Type II (7085 kDa), and Type III (250-350 kDa). The Type III receptor, a proteoglycan that exists in membranebound and soluble forms, binds TGFbeta1, TGFbeta2, and TGFbeta3 but does not appear to be involved in signal transduction. The Type II receptor is a membrane bound serine/threonine kinase that binds TGFbeta1 and TGFbeta3 with high affinity and TGFbeta2 with a much lower affinity. The Type I receptor, originally known as ALK5 (Activin receptor-like kinase) is also a membranebound serine/threonine kinase that apparently requires the presence of the Type II receptor to bind TGFbeta. Current evidence suggests that signal transduction requires the cytoplasmic domains of both the Type I and Type II receptors.

Western Blot (WB), Immunohistochemistry (IHC)

1. Western blot: Yes (1:800-2000) 2. Immunohistochemistry (Paraffin): Yes (1:50-100)

transforming growth factor, beta receptor I

TGF-beta receptor type-1; ESK2; TGFR-1; TGF-beta receptor type I; transforming growth factor-beta receptor type I

TGF-beta receptor type-1

TGFR-1; TGF-beta receptor type I; TbetaR-I??[Similar Products]

TGFR1_MOUSE

This gene encodes a member of the transforming growth factor beta (TGF-beta) receptor family of proteins. These proteins comprise one component of the TGF-beta signaling pathway, which transduces extracellular signals into gene expression changes to regulate a wide range of cellular responses, including proliferation, migration, differentiation and apoptosis. Homozygous knockout mice for this gene exhibit impaired angiogenesis and embryonic lethality. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2015]

Function: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation

By similarity.

Catalytic activity: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactor: Magnesium or manganese

By similarity.

Enzyme regulation: Kept in an inactive conformation by FKBP1A preventing receptor activation in absence of ligand. CD109 is another inhibitor of the receptor

By similarity.

Subunit structure: Homodimer; in the endoplasmic reticulum but also at the cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with CD109; inhibits TGF-beta receptor activation in keratinocytes. Interacts with RBPMS. Interacts (unphosphorylated) with FKBP1A; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with TRAF6 and MAP3K7; induces MAP3K7 activation by TRAF6. Interacts with PARD6A; involved in TGF-beta induced epithelial to mesenchymal transition. Interacts with SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1 and SMURF2 to the TGF-beta receptor

By similarity. Interacts with USP15 and VPS39

By similarity.

Subcellular location: Cell membrane; Single-pass type I membrane protein

By similarity. Cell junction ? tight junction

By similarity.

Post-translational modification: Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding

By similarity.N-Glycosylated

By similarity.Ubiquitinated; undergoes ubiquitination catalyzed by several E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the proteasomal and/or lysosomal degradation of the receptor thereby negatively regulating its activity. Deubiquitinated by USP15, leading to stabilization of the protein and enhanced TGF-beta signal

By similarity.

Sequence similarities: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.Contains 1 GS domain.Contains 1 protein kinase domain.

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