CD29 antibody | JB1B
Mouse anti Human CD29 antibody, clone JB1B has been successfully employed for the detection of porcine CD29 in formalin fixed, paraffin embedded material (Papageorgiou et al. 2014) and also to stimulate the adherence of several cell types (Wilkins et al. 1996).
The removal of azide is recommended prior to use in functional assays.
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Pig Cynomolgus monkey Rhesus Monkey Rat
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide
- Purified Human beta1 integrin
- Approx. Protein Concentrations
- Ig concentration 0.5 mg/ml
- Fusion Partners
- Spleen cells from immunized BALB/c mice were fused with cells of the NS1 mouse myeloma cell line.
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
- 12 months from date of despatch
Applications of CD29 antibody
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Frozen||5ug/ml|
Secondary Antibodies Available
Negative Isotype Controls Available
|Description||Product Code||Applications||Pack Size||List Price||Quantity|
|Mouse IgG2a Negative Control||MCA929||F||100 Tests|
Product Specific References
References for CD29 antibody
Stupack, D.G. et al. (1994) Control of lymphocyte integrin function: evidence for multiple contributing factors.
Cell Immunol. 155 (1): 237-45.
Wilkins, J.A. et al. (1996) Control of beta1 integrin function. Localization of stimulatory epitopes.
J Biol Chem. 271 (6): 3046-51.
Yoshino N et al. (2000) Upgrading of flow cytometric analysis for absolute counts, cytokines and other antigenic molecules of cynomolgus monkeys (Macaca fascicularis) by using anti-human cross-reactive antibodies.
Exp Anim. 49 (2): 97-110.
Batista da Silva, A.P. et al. (2004) The major outer sheath protein of Treponema denticola inhibits the binding step of collagen phagocytosis in fibroblasts.
Cell Microbiol. 6: 485-98.
Levite, M. et al. (2000) Extracellular K(+) and opening of voltage-gated potassium channels activate T cell integrin function: physical and functional association between Kv1.3 channels and beta1 integrins.
J Exp Med. 191: 1167-76.
Bass, R. et al. (2005) Regulation of urokinase receptor proteolytic function by the tetraspanin CD82.
J Biol Chem. 280: 14811-8.
Clark, K. et al. (2000) Production of recombinant soluble human integrin alpha4beta1.
FEBS Lett. 471: 182-6.
Papageorgiou, I. et al. (2014) Interaction of micron and nano-sized particles with cells of the dura mater.
J Biomed Mater Res B Appl Biomater. 102 (7): 1496-505.
Takaki, T. (2006) Interferon-gamma inhibits collagen phagocytosis in human fibroblasts by inducing subcortical actin assembly and reducing ability of beta1 integrin to bind to collagen.
Inflamm Res. 55: 534-42.
Eirin A et al. (2017) Integrated transcriptomic and proteomic analysis of the molecular cargo of extracellular vesicles derived from porcine adipose tissue-derived mesenchymal stem cells.
PLoS One. 12 (3): e0174303.
Meng, Y. et al. (2018) The metabolic syndrome alters the miRNA signature of porcine adipose tissue-derived mesenchymal stem cells.
Cytometry A. 93 (1): 93-103.
Dawson, H.D. and Lunney, J.K. (2018) Porcine cluster of differentiation (CD) markers 2018 update.
Res Vet Sci. 118: 199-246.
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