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AB106092

Anti-Smad1 (phospho S206) antibody

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(1 Publication)

Rabbit Polyclonal SMAD1 phospho S206 antibody. Suitable for WB, ELISA and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human SMAD1 phospho S206.

View Alternative Names

BSP1, MADH1, MADR1, SMAD1, Mothers against decapentaplegic homolog 1, MAD homolog 1, Mothers against DPP homolog 1, JV4-1, Mad-related protein 1, SMAD family member 1, Transforming growth factor-beta-signaling protein 1, SMAD 1, Smad1, hSMAD1, BSP-1

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ELISA, WB

applications

Immunogen

Synthetic Peptide within Human SMAD1 phospho S206. The exact immunogen used to generate this antibody is proprietary information.

Q15797

Specificity

This affinity-purified antibody is directed against the phosphorylated form of human SMAD1 protein at the pS206 residue. Reactivity occurs against human SMAD1 pS206 protein and the antibody is specific for the phosphorylated form of the protein. Reactivity with non-phosphorylated human SMAD1 is minimal by ELISA and western blot. A BLAST analysis was used to suggest 100% cross reactivity with SMAD1 from human, Duckbill platypus, Drosophila, mouse, opossum, chimpanzee, bonobo, orangutan, gorilla, macaque, cattle, sheep, pig, rat, horse, salmon, chicken, and dog based on the sequence homology with the immunogen. Reactivity against homologues from other sources is not known.

Reactivity data

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Product details

Expiration date is one year from date of opening. Dilute only prior to immediate use.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification
Purification notes
ab106092 was affinity purified from monospecific antiserum by immunoaffinity purification. Antiserum was first purified against the phosphorylated form of the immunizing peptide. The resultant affinity purified antibody was then cross adsorbed against the non-phosphorylated form of the immunizing peptide.
Storage buffer
pH: 7.2 Preservative: 0.01% Sodium azide Constituents: 0.88% Sodium chloride, 0.424% Potassium phosphate solution
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Smad1 also known as Mothers against decapentaplegic homolog 1 (MADH1) is a protein encoded by the SMAD1 gene in humans. It has a molecular mass of approximately 53 kDa and functions as a receptor-regulated Smad protein. Smad1 primarily transmits signals from the bone morphogenetic proteins (BMPs) a group of growth factors and cytokines. Expression of Smad1 occurs in various tissues including the lung heart and kidney. It plays an important role in mediating signaling pathways within different cellular environments.
Biological function summary

Smad1 participates in the transmission of BMP signals from the cell surface to the nucleus ensuring transcriptional regulation of target genes. In the presence of BMPs Smad1 forms complexes with Smad4 upon activation. These Smad complexes then translocate to the nucleus where they regulate gene expression. Smad1 influences cellular responses such as proliferation differentiation and apoptosis. In particular it plays a significant role in bone development and osteogenesis.

Pathways

Smad1 plays an important role within the BMP signaling pathway which is important for early development and tissue homeostasis. Within this pathway BMPs trigger the phosphorylation of Smad1 which then associates with Smad4 to propagate downstream signaling. Another associated pathway includes the TGF-beta signaling pathway where Smads like Smad2 and Smad3 show functional similarities and differences with Smad1. The interactions of Smad1 with related proteins like Smad4 highlight its significant contribution to cellular processes regulated by these pathways.

Smad1 associates with various pathological conditions. For instance aberrant Smad1 signaling has implications in cancer particularly in processes like tumor progression and metastasis. Disruptions in the BMP pathway involving Smad1 and Smad4 can influence the onset and development of disorders such as pulmonary hypertension where inappropriate cell growth and remodeling occur. Understanding Smad1's role in these contexts provides insights into potential therapeutic avenues for treatment and management of these conditions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Transcriptional modulator that plays a role in various cellular processes, including embryonic development, cell differentiation, and tissue homeostasis (PubMed : 9335504). Upon BMP ligand binding to their receptors at the cell surface, is phosphorylated by activated type I BMP receptors (BMPRIs) and associates with SMAD4 to form a heteromeric complex which translocates into the nucleus acting as transcription factor (PubMed : 33667543). In turn, the hetero-trimeric complex recognizes cis-regulatory elements containing Smad Binding Elements (SBEs) to modulate the outcome of the signaling network (PubMed : 33667543). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Positively regulates BMP4-induced expression of odontogenic development regulator MSX1 following IPO7-mediated nuclear import (By similarity).
See full target information SMAD1 phospho S206

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

The journal of gene medicine 25:e3552 PubMed37337736

2023

B4GALNT1 promotes carcinogenesis by regulating epithelial-mesenchymal transition in hepatocellular carcinoma based on pan-cancer analysis.

Applications

Unspecified application

Species

Unspecified reactive species

Wenli Liu,Yutong Chen,Jinqiang Yang,Mingliang Guo,Li Wang
View all publications

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