JunD Antibody [K7H15] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Lane 1: C6, Lane 2: 3T3, Lane 3: 293T, Lane 4: Jurkat

Usage Information

Dilution
WB1:1000 IHC1:1000 IF1:10000

Application
WB, IHC, IF

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
35 kDa 39 kDa,42 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human fetal brain; Human fetal liver; Human mammary gland tissue; Human fetal heart; Human lung squamous cell carcinoma tissue; Mouse cerebral cortex tissue; Rat cerebral cortex tissue; Human fetal kidney; HeLa cells; 293T cells; Jurkat cells; Raw264.7 cells; PC12 cells; NIH 3T3 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
JunD Antibody [K7H15] detects endogenous levels of total JunD protein.

Clone
K7H15

Synonym(s)
Transcription factor JunD; Transcription factor AP-1 subunit JunD; JUND

Background
JunD is the most stable and least homologous AP-1 family bZIP transcription factor. It contains N-terminal transactivation domains A1 and A2 with JNK/SAPK phospho-acceptor sites (Ser69, Thr89, Thr91) that regulate activity in response to stress and growth factors. The protein has a divergent transrepression δ domain that enables anti-proliferative dominance, and a C-terminal bZIP module consisting of a basic region that inserts into the TGAGTCA TRE major groove and a leucine zipper that forms Y-shaped α-helical dimers with FosB, ATF2, or CREB. JunD:Fos heterodimers can displace c-Jun from proliferative TREs, repressing genes like cyclin D1 and p16^INK4a in Ras-transformed cells via δ domain steric occlusion, while also activating antioxidant and DNA repair/apoptosis genes such as VEGF and GADD45α/γ. The intronless junD gene allows rapid production of the ΔJunD splice variant, which lacks A1 and is less efficiently phosphorylated by JNK, resulting in weaker activation. JunD binds CREB sites in its own promoter to repress ZO-1 transcription and translation, destabilizing mRNA via 3'UTR-TIAR interaction and weakening epithelial barrier integrity. JunD knockout mice are viable but exhibit cardiomyocyte hypertrophy from derepressed IGF-I/ERK, stunted long-bone growth due to VEGF/FGF deficits, and infertility. Somatic amplification of JunD drives androgen-independent prostate cancer through AR crosstalk and restrains senescence in fibroblasts. Knockdown of JunD induces GADD45-mediated apoptosis and reduces prostate cancer xenograft growth.

Background

JunD is the most stable and least homologous AP-1 family bZIP transcription factor. It contains N-terminal transactivation domains A1 and A2 with JNK/SAPK phospho-acceptor sites (Ser69, Thr89, Thr91) that regulate activity in response to stress and growth factors. The protein has a divergent transrepression δ domain that enables anti-proliferative dominance, and a C-terminal bZIP module consisting of a basic region that inserts into the TGAGTCA TRE major groove and a leucine zipper that forms Y-shaped α-helical dimers with FosB, ATF2, or CREB. JunD:Fos heterodimers can displace c-Jun from proliferative TREs, repressing genes like cyclin D1 and p16^INK4a in Ras-transformed cells via δ domain steric occlusion, while also activating antioxidant and DNA repair/apoptosis genes such as VEGF and GADD45α/γ. The intronless junD gene allows rapid production of the ΔJunD splice variant, which lacks A1 and is less efficiently phosphorylated by JNK, resulting in weaker activation. JunD binds CREB sites in its own promoter to repress ZO-1 transcription and translation, destabilizing mRNA via 3'UTR-TIAR interaction and weakening epithelial barrier integrity. JunD knockout mice are viable but exhibit cardiomyocyte hypertrophy from derepressed IGF-I/ERK, stunted long-bone growth due to VEGF/FGF deficits, and infertility. Somatic amplification of JunD drives androgen-independent prostate cancer through AR crosstalk and restrains senescence in fibroblasts. Knockdown of JunD induces GADD45-mediated apoptosis and reduces prostate cancer xenograft growth.

References
https://pubmed.ncbi.nlm.nih.gov/18427548/ https://pubmed.ncbi.nlm.nih.gov/18562690/

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%