TGF β1 Antibody (Rabbit mAb) [N23L9]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:5000

Application
WB

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
44 kDa 12 kDa, 48 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Mouse serum; Mouse spleen; Rat kidney; Rat spleen; Rat serum; Human kidney; Human spleen; Mouse spleen tissue lysate; Rat spleen tissue lysate; Mouse heart tissue lysate; L-929 cells; RAW 264.7 cells; A549 cells; HL-60 cells; K-562 cells; NIH/3T3 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
TGF β1 Antibody (Rabbit mAb) [N23L9] detects endogenous levels of total TGF β1 protein.

Clone
N23L9

Synonym(s)
TGFB, TGFB1, Transforming growth factor beta-1 proprotein

Background
TGF-β1 belongs to the transforming growth factor-β superfamily of secreted cytokines and is synthesized as a proprotein cleaved by furin into two non-covalently associated chains, the latency-associated peptide and mature TGF-β1, which together form a ring-shaped latent complex that sterically shields the growth factor from receptor engagement. This latent complex is tethered within the extracellular matrix through disulfide-linked association with latent TGF-β binding proteins, holding TGF-β1 in an inactive, storage-competent state until a local activation signal is received. Activation requires αv integrins binding an RGD motif within the latency-associated peptide and exerting mechanical force on this domain, a process resisted by the matrix anchoring of the latent complex, and this force-dependent unfastening deforms the prodomain sufficiently to expose the receptor-binding surface of mature TGF-β1 without necessarily releasing it from the complex entirely. Once accessible, TGF-β1 binds the constitutively active type II receptor, TGFBR2, which recruits and trans-phosphorylates the type I receptor, TGFBR1, on serine residues within its juxtamembrane GS domain. Activated TGFBR1 then phosphorylates SMAD2 and SMAD3 at two C-terminal serine residues, triggering their dissociation from the receptor complex and association with SMAD4 to form a heteromeric complex that translocates to the nucleus and regulates transcription of TGF-β1 target genes. Distinct phosphorylation patterns on the SMAD2/3 linker versus C-terminal regions determine whether downstream signaling favors cytostatic, mitogenic, or fibrogenic transcriptional outcomes, giving the pathway context-dependent functional flexibility despite a shared core receptor mechanism. Because activation is restricted to sites where integrin engagement and mechanical force converge, TGF-β1 signaling remains highly localized despite broad tissue-level expression, a regulatory feature that governs bone formation, T-helper 17 versus regulatory T-cell lineage commitment, and epithelial-to-mesenchymal transition, and whose dysregulation contributes to fibrotic and immune-related disease.

Background

TGF-β1 belongs to the transforming growth factor-β superfamily of secreted cytokines and is synthesized as a proprotein cleaved by furin into two non-covalently associated chains, the latency-associated peptide and mature TGF-β1, which together form a ring-shaped latent complex that sterically shields the growth factor from receptor engagement. This latent complex is tethered within the extracellular matrix through disulfide-linked association with latent TGF-β binding proteins, holding TGF-β1 in an inactive, storage-competent state until a local activation signal is received. Activation requires αv integrins binding an RGD motif within the latency-associated peptide and exerting mechanical force on this domain, a process resisted by the matrix anchoring of the latent complex, and this force-dependent unfastening deforms the prodomain sufficiently to expose the receptor-binding surface of mature TGF-β1 without necessarily releasing it from the complex entirely. Once accessible, TGF-β1 binds the constitutively active type II receptor, TGFBR2, which recruits and trans-phosphorylates the type I receptor, TGFBR1, on serine residues within its juxtamembrane GS domain. Activated TGFBR1 then phosphorylates SMAD2 and SMAD3 at two C-terminal serine residues, triggering their dissociation from the receptor complex and association with SMAD4 to form a heteromeric complex that translocates to the nucleus and regulates transcription of TGF-β1 target genes. Distinct phosphorylation patterns on the SMAD2/3 linker versus C-terminal regions determine whether downstream signaling favors cytostatic, mitogenic, or fibrogenic transcriptional outcomes, giving the pathway context-dependent functional flexibility despite a shared core receptor mechanism. Because activation is restricted to sites where integrin engagement and mechanical force converge, TGF-β1 signaling remains highly localized despite broad tissue-level expression, a regulatory feature that governs bone formation, T-helper 17 versus regulatory T-cell lineage commitment, and epithelial-to-mesenchymal transition, and whose dysregulation contributes to fibrotic and immune-related disease.

References
https://pubmed.ncbi.nlm.nih.gov/21677751/ https://pubmed.ncbi.nlm.nih.gov/22617150/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%